Pub Date : 1996-06-01DOI: 10.1128/mr.60.2.316-341.1996
B Henderson, S Poole, M Wilson
Cytokines are a diverse group of proteins and glycoproteins which have potent and wide-ranging effects on eukaryotic cell function and are now recognized as important mediators of tissue pathology in infectious diseases. It is increasingly recognized that for many bacterial species, cytokine induction is a major virulence mechanism. Until recent years, the only bacterial component known to stimulate cytokine synthesis was lipopolysaccharide (LPS). It is only within the past decade that it has been clearly shown that many components associated with the bacterial cell wall, including proteins, glycoproteins, lipoproteins, carbohydrates, and lipids, have the capacity to stimulate mammalian cells to produce a diverse array of cytokines. It has been established that many of these cytokine-inducing molecules act by mechanisms distinct from that of LPS, and thus their activities are not due to LPS contamination. Bacteria produce a wide range of virulence factors which cause host tissue pathology, and these diverse factors have been grouped into four families: adhesins, aggressins, impedins, and invasins. We suggest that the array of bacterial cytokine-inducing molecules represents a new class of bacterial virulence factor, and, by analogy with the known virulence families, we suggest the term "modulin" to describe these molecules, because the action of cytokines is to modulate eukaryotic cell behavior. This review summarizes our current understanding of cytokine biology in relation to tissue homeostasis and disease and concisely reviews the current literature on the cytokine-inducing molecules produced by gram-negative and gram-positive bacteria, with an emphasis on the cellular mechanisms responsible for cytokine induction. We propose that modulins, by controlling the host immune and inflammatory responses, maintain the large commensal flora that all multicellular organisms support.
{"title":"Bacterial modulins: a novel class of virulence factors which cause host tissue pathology by inducing cytokine synthesis.","authors":"B Henderson, S Poole, M Wilson","doi":"10.1128/mr.60.2.316-341.1996","DOIUrl":"https://doi.org/10.1128/mr.60.2.316-341.1996","url":null,"abstract":"<p><p>Cytokines are a diverse group of proteins and glycoproteins which have potent and wide-ranging effects on eukaryotic cell function and are now recognized as important mediators of tissue pathology in infectious diseases. It is increasingly recognized that for many bacterial species, cytokine induction is a major virulence mechanism. Until recent years, the only bacterial component known to stimulate cytokine synthesis was lipopolysaccharide (LPS). It is only within the past decade that it has been clearly shown that many components associated with the bacterial cell wall, including proteins, glycoproteins, lipoproteins, carbohydrates, and lipids, have the capacity to stimulate mammalian cells to produce a diverse array of cytokines. It has been established that many of these cytokine-inducing molecules act by mechanisms distinct from that of LPS, and thus their activities are not due to LPS contamination. Bacteria produce a wide range of virulence factors which cause host tissue pathology, and these diverse factors have been grouped into four families: adhesins, aggressins, impedins, and invasins. We suggest that the array of bacterial cytokine-inducing molecules represents a new class of bacterial virulence factor, and, by analogy with the known virulence families, we suggest the term \"modulin\" to describe these molecules, because the action of cytokines is to modulate eukaryotic cell behavior. This review summarizes our current understanding of cytokine biology in relation to tissue homeostasis and disease and concisely reviews the current literature on the cytokine-inducing molecules produced by gram-negative and gram-positive bacteria, with an emphasis on the cellular mechanisms responsible for cytokine induction. We propose that modulins, by controlling the host immune and inflammatory responses, maintain the large commensal flora that all multicellular organisms support.</p>","PeriodicalId":18499,"journal":{"name":"Microbiological reviews","volume":"60 2","pages":"316-41"},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC239446/pdf/600316.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19772644","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1996-06-01DOI: 10.1128/MMBR.60.2.366-385.1996
P. S. Lovett, E. J. Rogers
Studies of bacterial and eukaryotic systems have identified two-gene operons in which the translation product of the upstream gene influences translation of the downstream gene. The upstream gene, referred to as a leader (gene) in bacterial systems or an upstream open reading frame (uORF) in eukaryotes, encodes a peptide that interferes with a function(s) of its translating ribosome. The peptides are therefore cis-acting negative regulators of translation. The inhibitory peptides typically consist of fewer than 25 residues and function prior to emergence from the ribosome. A biological role for this class of translation inhibitor is demonstrated in translation attenuation, a form or regulation that controls the inducible translation of the chloramphenicol resistance genes cat and cmlA in bacteria. Induction of cat or cmlA requires ribosome stalling at a particular codon in the leader region of the mRNA. Stalling destabilizes an adjacent, downstream mRNA secondary structure that normally sequesters the ribosome-binding site for the cat or cmlA coding regions. Genetic studies indicate that the nascent, leader-encoded peptide is the selector of the site of ribosome stalling in leader mRNA by cis interference with translation. Synthetic leader peptides inhibit ribosomal peptidyltransferase in vitro, leading to the prediction that this activity is the basis for stall site selection. Recent studies have shown that the leader peptides are rRNA-binding peptides with targets at the peptidyl transferase center of 23S rRNA. uORFs associated with several eukaryotic genes inhibit downstream translation. When inhibition depends on the specific codon sequence of the uORF, it has been proposed that the uORF-encoded nascent peptide prevents ribosome release from the mRNA at the uORF stop codon. This sets up a blockade to ribosome scanning which minimizes downstream translation. Segments within large proteins also appear to regulate ribosome activity in cis, although in most of the known examples the active amino acid sequences function after their emergence from the ribosome, cis control of translation by the nascent peptide is gene specific; nearly all such regulatory peptides exert no obvious trans effects in cells. The in vitro biochemical activities of the cat/cmla leader peptides on ribosomes and rRNA suggest a mechanism through which the nascent peptide can modify ribosome behavior. Other cis-acting regulatory peptides may involve more complex ribosomal interactions.
{"title":"Ribosome regulation by the nascent peptide.","authors":"P. S. Lovett, E. J. Rogers","doi":"10.1128/MMBR.60.2.366-385.1996","DOIUrl":"https://doi.org/10.1128/MMBR.60.2.366-385.1996","url":null,"abstract":"Studies of bacterial and eukaryotic systems have identified two-gene operons in which the translation product of the upstream gene influences translation of the downstream gene. The upstream gene, referred to as a leader (gene) in bacterial systems or an upstream open reading frame (uORF) in eukaryotes, encodes a peptide that interferes with a function(s) of its translating ribosome. The peptides are therefore cis-acting negative regulators of translation. The inhibitory peptides typically consist of fewer than 25 residues and function prior to emergence from the ribosome. A biological role for this class of translation inhibitor is demonstrated in translation attenuation, a form or regulation that controls the inducible translation of the chloramphenicol resistance genes cat and cmlA in bacteria. Induction of cat or cmlA requires ribosome stalling at a particular codon in the leader region of the mRNA. Stalling destabilizes an adjacent, downstream mRNA secondary structure that normally sequesters the ribosome-binding site for the cat or cmlA coding regions. Genetic studies indicate that the nascent, leader-encoded peptide is the selector of the site of ribosome stalling in leader mRNA by cis interference with translation. Synthetic leader peptides inhibit ribosomal peptidyltransferase in vitro, leading to the prediction that this activity is the basis for stall site selection. Recent studies have shown that the leader peptides are rRNA-binding peptides with targets at the peptidyl transferase center of 23S rRNA. uORFs associated with several eukaryotic genes inhibit downstream translation. When inhibition depends on the specific codon sequence of the uORF, it has been proposed that the uORF-encoded nascent peptide prevents ribosome release from the mRNA at the uORF stop codon. This sets up a blockade to ribosome scanning which minimizes downstream translation. Segments within large proteins also appear to regulate ribosome activity in cis, although in most of the known examples the active amino acid sequences function after their emergence from the ribosome, cis control of translation by the nascent peptide is gene specific; nearly all such regulatory peptides exert no obvious trans effects in cells. The in vitro biochemical activities of the cat/cmla leader peptides on ribosomes and rRNA suggest a mechanism through which the nascent peptide can modify ribosome behavior. Other cis-acting regulatory peptides may involve more complex ribosomal interactions.","PeriodicalId":18499,"journal":{"name":"Microbiological reviews","volume":"18 3","pages":"366-85"},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91529192","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1996-06-01DOI: 10.1128/mr.60.2.439-471.1996
R S Hanson, T E Hanson
Methane-utilizing bacteria (methanotrophs) are a diverse group of gram-negative bacteria that are related to other members of the Proteobacteria. These bacteria are classified into three groups based on the pathways used for assimilation of formaldehyde, the major source of cell carbon, and other physiological and morphological features. The type I and type X methanotrophs are found within the gamma subdivision of the Proteobacteria and employ the ribulose monophosphate pathway for formaldehyde assimilation, whereas type II methanotrophs, which employ the serine pathway for formaldehyde assimilation, form a coherent cluster within the beta subdivision of the Proteobacteria. Methanotrophic bacteria are ubiquitous. The growth of type II bacteria appears to be favored in environments that contain relatively high levels of methane, low levels of dissolved oxygen, and limiting concentrations of combined nitrogen and/or copper. Type I methanotrophs appear to be dominant in environments in which methane is limiting and combined nitrogen and copper levels are relatively high. These bacteria serve as biofilters for the oxidation of methane produced in anaerobic environments, and when oxygen is present in soils, atmospheric methane is oxidized. Their activities in nature are greatly influenced by agricultural practices and other human activities. Recent evidence indicates that naturally occurring, uncultured methanotrophs represent new genera. Methanotrophs that are capable of oxidizing methane at atmospheric levels exhibit methane oxidation kinetics different from those of methanotrophs available in pure cultures. A limited number of methanotrophs have the genetic capacity to synthesize a soluble methane monooxygenase which catalyzes the rapid oxidation of environmental pollutants including trichloroethylene.
{"title":"Methanotrophic bacteria.","authors":"R S Hanson, T E Hanson","doi":"10.1128/mr.60.2.439-471.1996","DOIUrl":"https://doi.org/10.1128/mr.60.2.439-471.1996","url":null,"abstract":"<p><p>Methane-utilizing bacteria (methanotrophs) are a diverse group of gram-negative bacteria that are related to other members of the Proteobacteria. These bacteria are classified into three groups based on the pathways used for assimilation of formaldehyde, the major source of cell carbon, and other physiological and morphological features. The type I and type X methanotrophs are found within the gamma subdivision of the Proteobacteria and employ the ribulose monophosphate pathway for formaldehyde assimilation, whereas type II methanotrophs, which employ the serine pathway for formaldehyde assimilation, form a coherent cluster within the beta subdivision of the Proteobacteria. Methanotrophic bacteria are ubiquitous. The growth of type II bacteria appears to be favored in environments that contain relatively high levels of methane, low levels of dissolved oxygen, and limiting concentrations of combined nitrogen and/or copper. Type I methanotrophs appear to be dominant in environments in which methane is limiting and combined nitrogen and copper levels are relatively high. These bacteria serve as biofilters for the oxidation of methane produced in anaerobic environments, and when oxygen is present in soils, atmospheric methane is oxidized. Their activities in nature are greatly influenced by agricultural practices and other human activities. Recent evidence indicates that naturally occurring, uncultured methanotrophs represent new genera. Methanotrophs that are capable of oxidizing methane at atmospheric levels exhibit methane oxidation kinetics different from those of methanotrophs available in pure cultures. A limited number of methanotrophs have the genetic capacity to synthesize a soluble methane monooxygenase which catalyzes the rapid oxidation of environmental pollutants including trichloroethylene.</p>","PeriodicalId":18499,"journal":{"name":"Microbiological reviews","volume":"60 2","pages":"439-71"},"PeriodicalIF":0.0,"publicationDate":"1996-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC239451/pdf/600439.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19771851","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1996-03-01DOI: 10.1128/mr.60.1.167-215.1996
C L Sears, J B Kaper
{"title":"Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion.","authors":"C L Sears, J B Kaper","doi":"10.1128/mr.60.1.167-215.1996","DOIUrl":"https://doi.org/10.1128/mr.60.1.167-215.1996","url":null,"abstract":"","PeriodicalId":18499,"journal":{"name":"Microbiological reviews","volume":"60 1","pages":"167-215"},"PeriodicalIF":0.0,"publicationDate":"1996-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC239424/pdf/600167.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19821029","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1996-03-01DOI: 10.1128/MMBR.60.1.233-249.1996
G. Caponigro, Roy Parker
INTRODUCTION 233 METHODS FOR STUDYING mRNA TURNOVER IN S. CEREVISIAE 234 Approach to Steady-State Labeling 234 Inhibition of Transcription by Using Drugs 234 Inhibition of Transcription by Using a Conditional Allele of RNA Polymerase II 234 Inhibition of Transcription by Using Regulated Promoters 235 Transcriptional Pulse-Chase: a Method for Examining Pathways of Decay 235 Identification of Intermediates in mRNA Decay 235 DETERMINANTS OF mRNA STABILITY IN S. CEREVISIAE 236 Specific Sequences Influence mRNA Half-Lives 236 Nonspecific Features of mRNAs Generally Do Not Influence mRNA Half-Lives 237 There is no correlation between mRNA length and stability 237 Ribosome protection cannot account for mRNA half-lives 237 Rare codons are not general determinants of mRNA stability 238 A COMMON PATHWAY OF mRNA DECAY 238 Deadenylation Precedes the Decay of Some Yeast mRNAs 238 Decapping and 5*-to-3* Exonucleolytic Digestion Follow Deadenylation of Some Yeast mRNAs 239 Deadenylation-Dependent Decapping Is a Common Pathway of mRNA Decay 239 Control of mRNA Half-Lives through the Deadenylation-Dependent Decapping Pathway 240 Control of mRNA deadenylation 240 (i) Poly(A)-binding protein influences deadenylation 240 (ii) Poly(A)-binding protein-dependent nuclease activity from S. cerevisiae 240 (iii) Other proteins possibly involved in deadenylation 240 (iv) Models of poly(A) shortening 240 (v) Terminal deadenylation is not a rate-determining step for 5*-to-3* decay 241 Control of mRNA decapping 241 (i) The Pab1p-poly(A) tail complex inhibits mRNA decapping 241 (ii) Control of decapping after deadenylation 242 (iii) Decapping activities from S. cerevisiae 242 (iv) Translation and mRNA decapping 242 ADDITIONAL PATHWAYS OF mRNA DECAY IN S. CEREVISIAE 243 3*-to-5* mRNA Decay 243 Endonucleolytic Cleavage of mRNAs 243 mRNA Surveillance: Rapid Deadenylation-Independent Decapping 243 Early nonsense codons trigger mRNA decapping 243 Recognition of early nonsense codons 244 (i) Specific sequences are required 3* of early nonsense codons 244 (ii) Specific upstream elements partially block nonsense codon-mediated decay 245 trans-Acting factors in nonsense codon-mediated mRNA decay 245 Where in the cell does recognition of an early nonsense codon occur? 246 REGULATED mRNA TURNOVER IN S. CEREVISIAE 246 CONCLUSIONS 246 REFERENCES 246
{"title":"Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae.","authors":"G. Caponigro, Roy Parker","doi":"10.1128/MMBR.60.1.233-249.1996","DOIUrl":"https://doi.org/10.1128/MMBR.60.1.233-249.1996","url":null,"abstract":"INTRODUCTION 233 METHODS FOR STUDYING mRNA TURNOVER IN S. CEREVISIAE 234 Approach to Steady-State Labeling 234 Inhibition of Transcription by Using Drugs 234 Inhibition of Transcription by Using a Conditional Allele of RNA Polymerase II 234 Inhibition of Transcription by Using Regulated Promoters 235 Transcriptional Pulse-Chase: a Method for Examining Pathways of Decay 235 Identification of Intermediates in mRNA Decay 235 DETERMINANTS OF mRNA STABILITY IN S. CEREVISIAE 236 Specific Sequences Influence mRNA Half-Lives 236 Nonspecific Features of mRNAs Generally Do Not Influence mRNA Half-Lives 237 There is no correlation between mRNA length and stability 237 Ribosome protection cannot account for mRNA half-lives 237 Rare codons are not general determinants of mRNA stability 238 A COMMON PATHWAY OF mRNA DECAY 238 Deadenylation Precedes the Decay of Some Yeast mRNAs 238 Decapping and 5*-to-3* Exonucleolytic Digestion Follow Deadenylation of Some Yeast mRNAs 239 Deadenylation-Dependent Decapping Is a Common Pathway of mRNA Decay 239 Control of mRNA Half-Lives through the Deadenylation-Dependent Decapping Pathway 240 Control of mRNA deadenylation 240 (i) Poly(A)-binding protein influences deadenylation 240 (ii) Poly(A)-binding protein-dependent nuclease activity from S. cerevisiae 240 (iii) Other proteins possibly involved in deadenylation 240 (iv) Models of poly(A) shortening 240 (v) Terminal deadenylation is not a rate-determining step for 5*-to-3* decay 241 Control of mRNA decapping 241 (i) The Pab1p-poly(A) tail complex inhibits mRNA decapping 241 (ii) Control of decapping after deadenylation 242 (iii) Decapping activities from S. cerevisiae 242 (iv) Translation and mRNA decapping 242 ADDITIONAL PATHWAYS OF mRNA DECAY IN S. CEREVISIAE 243 3*-to-5* mRNA Decay 243 Endonucleolytic Cleavage of mRNAs 243 mRNA Surveillance: Rapid Deadenylation-Independent Decapping 243 Early nonsense codons trigger mRNA decapping 243 Recognition of early nonsense codons 244 (i) Specific sequences are required 3* of early nonsense codons 244 (ii) Specific upstream elements partially block nonsense codon-mediated decay 245 trans-Acting factors in nonsense codon-mediated mRNA decay 245 Where in the cell does recognition of an early nonsense codon occur? 246 REGULATED mRNA TURNOVER IN S. CEREVISIAE 246 CONCLUSIONS 246 REFERENCES 246","PeriodicalId":18499,"journal":{"name":"Microbiological reviews","volume":"46 1","pages":"233-49"},"PeriodicalIF":0.0,"publicationDate":"1996-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74127720","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1996-03-01DOI: 10.1128/mr.60.1.151-166.1996
T R Neu
INTRODUCTION AND TERMINOLOGY .............................................................................................................151 TYPES OF BACTERIAL SACs.................................................................................................................................153 SYNTHETIC SACs AND BACTERIA......................................................................................................................154 In Solution ...............................................................................................................................................................154 Sodium dodecyl sulfate ......................................................................................................................................154 Quaternary ammonium compounds.................................................................................................................154 Various surfactants.............................................................................................................................................155 Immobilized on Surfaces .......................................................................................................................................155 Insolubilized quaternary ammonium compounds ..........................................................................................155 Insolubilized block copolymer surfactants ......................................................................................................155 Miscellaneous Effects .............................................................................................................................................156 BACTERIAL SACs AND BACTERIA ......................................................................................................................156 Physiological Roles .................................................................................................................................................156 Other Observations ................................................................................................................................................157 Applied Aspects of Bacterial SACs.......................................................................................................................157 SURFACE-ACTIVE APPROACH TO BACTERIAL ADHESION/DEADHESION............................................157 SIGNIFICANCE OF BACTERIAL SACs IN ADHESION TO INTERFACES ..................................................158 SACs Bound at the Bacterial Cell Surface .........................................................................................................158 Cell-bound biosurfactants..................................................................................................................................158 Cell-bound polymeric SACs....................................................................................................
{"title":"Significance of bacterial surface-active compounds in interaction of bacteria with interfaces.","authors":"T R Neu","doi":"10.1128/mr.60.1.151-166.1996","DOIUrl":"https://doi.org/10.1128/mr.60.1.151-166.1996","url":null,"abstract":"INTRODUCTION AND TERMINOLOGY .............................................................................................................151 TYPES OF BACTERIAL SACs.................................................................................................................................153 SYNTHETIC SACs AND BACTERIA......................................................................................................................154 In Solution ...............................................................................................................................................................154 Sodium dodecyl sulfate ......................................................................................................................................154 Quaternary ammonium compounds.................................................................................................................154 Various surfactants.............................................................................................................................................155 Immobilized on Surfaces .......................................................................................................................................155 Insolubilized quaternary ammonium compounds ..........................................................................................155 Insolubilized block copolymer surfactants ......................................................................................................155 Miscellaneous Effects .............................................................................................................................................156 BACTERIAL SACs AND BACTERIA ......................................................................................................................156 Physiological Roles .................................................................................................................................................156 Other Observations ................................................................................................................................................157 Applied Aspects of Bacterial SACs.......................................................................................................................157 SURFACE-ACTIVE APPROACH TO BACTERIAL ADHESION/DEADHESION............................................157 SIGNIFICANCE OF BACTERIAL SACs IN ADHESION TO INTERFACES ..................................................158 SACs Bound at the Bacterial Cell Surface .........................................................................................................158 Cell-bound biosurfactants..................................................................................................................................158 Cell-bound polymeric SACs....................................................................................................","PeriodicalId":18499,"journal":{"name":"Microbiological reviews","volume":"60 1","pages":"151-66"},"PeriodicalIF":0.0,"publicationDate":"1996-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC239423/pdf/600151.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19821020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1996-03-01DOI: 10.1128/MMBR.60.1.70-102.1996
M. Dworkin
INTRODUCTION .........................................................................................................................................................71 MOLECULAR PHYLOGENY.....................................................................................................................................71 SIGNALING ..................................................................................................................................................................71 A Signal ......................................................................................................................................................................71 B Signal ......................................................................................................................................................................74 C Signal......................................................................................................................................................................74 D Signal......................................................................................................................................................................75 E Signal ......................................................................................................................................................................75 Summary of Signaling..............................................................................................................................................76 OTHER EXTRACELLULAR DEVELOPMENTAL FACTORS .............................................................................76 Glucosamine, Phospholipase, Glycerol, and Autocides .......................................................................................76 INITIATION SIGNAL..................................................................................................................................................77 EXTRACELLULAR APPENDAGES ..........................................................................................................................77 Pili...............................................................................................................................................................................77 Fibrils .........................................................................................................................................................................77 FRUITING BODY FORMATION ..............................................................................................................................79 Cell Density ...............................................................................................................................................................79 Role of Motility .........................................................................................................................................................79 Aggre
{"title":"Recent advances in the social and developmental biology of the myxobacteria.","authors":"M. Dworkin","doi":"10.1128/MMBR.60.1.70-102.1996","DOIUrl":"https://doi.org/10.1128/MMBR.60.1.70-102.1996","url":null,"abstract":"INTRODUCTION .........................................................................................................................................................71 MOLECULAR PHYLOGENY.....................................................................................................................................71 SIGNALING ..................................................................................................................................................................71 A Signal ......................................................................................................................................................................71 B Signal ......................................................................................................................................................................74 C Signal......................................................................................................................................................................74 D Signal......................................................................................................................................................................75 E Signal ......................................................................................................................................................................75 Summary of Signaling..............................................................................................................................................76 OTHER EXTRACELLULAR DEVELOPMENTAL FACTORS .............................................................................76 Glucosamine, Phospholipase, Glycerol, and Autocides .......................................................................................76 INITIATION SIGNAL..................................................................................................................................................77 EXTRACELLULAR APPENDAGES ..........................................................................................................................77 Pili...............................................................................................................................................................................77 Fibrils .........................................................................................................................................................................77 FRUITING BODY FORMATION ..............................................................................................................................79 Cell Density ...............................................................................................................................................................79 Role of Motility .........................................................................................................................................................79 Aggre","PeriodicalId":18499,"journal":{"name":"Microbiological reviews","volume":"4 1","pages":"70-102"},"PeriodicalIF":0.0,"publicationDate":"1996-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74574821","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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