Pub Date : 2002-12-09DOI: 10.1002/3527600035.BPOL7009
A. Driessen, N. Nouwen, C. Does
Introduction Historical Outline Protein Targeting to the Translocase Signal Peptides Co-translational Protein Targeting Post-translational Protein Targeting Converging Targeting Pathways Translocase: A Multisubunit Integral Membrane Protein Complex SecA SecY SecE SecG SecD, SecF, and YajC Conserved Protein Translocases in Bacteria, Eukaryotes, and Archaea Role of Lipids in Protein Translocation Mechanism of Protein Translocation ATP-driven Translocation Proton Motive Force-driven Translocation Dynamics of the Protein-conducting Channel Regulation of Protein Translocation Outlook and Perspectives Acknowledgments Keywords: translocation; membranes; SecA; SecY; SecE; SecB; SecD; SecF; SRP
{"title":"Bacterial protein secretion and targeting","authors":"A. Driessen, N. Nouwen, C. Does","doi":"10.1002/3527600035.BPOL7009","DOIUrl":"https://doi.org/10.1002/3527600035.BPOL7009","url":null,"abstract":"Introduction \u0000Historical Outline \u0000Protein Targeting to the Translocase \u0000Signal Peptides \u0000Co-translational Protein Targeting \u0000Post-translational Protein Targeting \u0000Converging Targeting Pathways \u0000 \u0000 \u0000Translocase: A Multisubunit Integral Membrane Protein Complex \u0000SecA \u0000SecY \u0000SecE \u0000SecG \u0000SecD, SecF, and YajC \u0000Conserved Protein Translocases in Bacteria, Eukaryotes, and Archaea \u0000 \u0000 \u0000Role of Lipids in Protein Translocation \u0000Mechanism of Protein Translocation \u0000ATP-driven Translocation \u0000Proton Motive Force-driven Translocation \u0000Dynamics of the Protein-conducting Channel \u0000Regulation of Protein Translocation \u0000 \u0000 \u0000Outlook and Perspectives \u0000Acknowledgments \u0000 \u0000 \u0000Keywords: \u0000 \u0000translocation; \u0000membranes; \u0000SecA; \u0000SecY; \u0000SecE; \u0000SecB; \u0000SecD; \u0000SecF; \u0000SRP","PeriodicalId":165163,"journal":{"name":"Biopolymers Online","volume":"29 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2002-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"123210911","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 : 2002-12-09DOI: 10.1002/3527600035.BPOL7013
T. Schäfer, O. Kirk, T. Borchert, C. Fuglsang, S. Pedersen, S. Salmon, H. Olsen, Randy Deinhammer, H. Lund
Introduction Historical Outline Enzymes for the Detergent Industry Introduction History Overview of Enzymes Latest Innovations Future Perspectives Enzymes for the Starch Industry Introduction History Enzymes Latest Innovations Perspectives Enzymes for Biofuel Introduction History Enzymes and Latest Innovations Future Perspectives Enzymes for the Textile Industry Introduction History Enzymes Latest Innovations Enzymes for the Pulp and Paper Industry Introduction Overview of Selected Applications Enzymes Future Perspectives Enzymes for Organic Synthesis Introduction History Enzymes Latest Innovations Perspectives Enzymes for Processing of Fats and Oils Introduction History Enzymes Latest Innovations Perspectives Key Technologies for the Discovery of Industrial Enzymes Exploring Nature's Diversity Protein Optimization Conclusion Acknowledgments Keywords: industrial enzymes; starch; textile; detergent; fuel; fats; oil; organic synthesis; pulp and paper; diversity; screening; assay technology; molecular biology; protein engineering; rational protein design; directed evolution
{"title":"Enzymes for Technical Applications","authors":"T. Schäfer, O. Kirk, T. Borchert, C. Fuglsang, S. Pedersen, S. Salmon, H. Olsen, Randy Deinhammer, H. Lund","doi":"10.1002/3527600035.BPOL7013","DOIUrl":"https://doi.org/10.1002/3527600035.BPOL7013","url":null,"abstract":"Introduction \u0000Historical Outline \u0000Enzymes for the Detergent Industry \u0000Introduction \u0000History \u0000Overview of Enzymes \u0000Latest Innovations \u0000Future Perspectives \u0000 \u0000 \u0000Enzymes for the Starch Industry \u0000Introduction \u0000History \u0000Enzymes \u0000Latest Innovations \u0000Perspectives \u0000 \u0000 \u0000Enzymes for Biofuel \u0000Introduction \u0000History \u0000Enzymes and Latest Innovations \u0000Future Perspectives \u0000 \u0000 \u0000Enzymes for the Textile Industry \u0000Introduction \u0000History \u0000Enzymes \u0000Latest Innovations \u0000 \u0000 \u0000Enzymes for the Pulp and Paper Industry \u0000Introduction \u0000Overview of Selected Applications \u0000Enzymes \u0000Future Perspectives \u0000 \u0000 \u0000Enzymes for Organic Synthesis \u0000Introduction \u0000History \u0000Enzymes \u0000Latest Innovations \u0000Perspectives \u0000 \u0000 \u0000Enzymes for Processing of Fats and Oils \u0000Introduction \u0000History \u0000Enzymes \u0000Latest Innovations \u0000Perspectives \u0000 \u0000 \u0000Key Technologies for the Discovery of Industrial Enzymes \u0000Exploring Nature's Diversity \u0000Protein Optimization \u0000Conclusion \u0000 \u0000 \u0000Acknowledgments \u0000 \u0000 \u0000Keywords: \u0000 \u0000industrial enzymes; \u0000starch; \u0000textile; \u0000detergent; \u0000fuel; \u0000fats; \u0000oil; \u0000organic synthesis; \u0000pulp and paper; \u0000diversity; \u0000screening; \u0000assay technology; \u0000molecular biology; \u0000protein engineering; \u0000rational protein design; \u0000directed evolution","PeriodicalId":165163,"journal":{"name":"Biopolymers Online","volume":"12 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2002-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"130379755","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 : 2002-12-09DOI: 10.1002/3527600035.BPOL7014
S. Witt, W. Baumeister
Introduction: Controlling Intracellular Proteolysis Historical Outline Occurrence and Subunit Composition of 20S Proteasomes Structural Features of the 20S Proteasome Catalytic Mechanism of the 20S Proteasome Processing and Assembly of 20S Proteasomes Size Distribution of 20S Proteasome Products The 19S Regulatory Complex Subcomplexes and Subunits of the 19S Regulator The PA28 Activator Outlook and Perspectives Keywords: 20S/26S proteasome; 19S regulatory complex; protein degradation; ubiquitin; proteolysis; macromolecular assembly; Ntn hydrolases; PA28 activator
{"title":"Proteasomes: Molecular Machines for Protein Degradation","authors":"S. Witt, W. Baumeister","doi":"10.1002/3527600035.BPOL7014","DOIUrl":"https://doi.org/10.1002/3527600035.BPOL7014","url":null,"abstract":"Introduction: Controlling Intracellular Proteolysis \u0000Historical Outline \u0000Occurrence and Subunit Composition of 20S Proteasomes \u0000Structural Features of the 20S Proteasome \u0000Catalytic Mechanism of the 20S Proteasome \u0000Processing and Assembly of 20S Proteasomes \u0000Size Distribution of 20S Proteasome Products \u0000The 19S Regulatory Complex \u0000Subcomplexes and Subunits of the 19S Regulator \u0000The PA28 Activator \u0000Outlook and Perspectives \u0000 \u0000 \u0000Keywords: \u0000 \u000020S/26S proteasome; \u000019S regulatory complex; \u0000protein degradation; \u0000ubiquitin; \u0000proteolysis; \u0000macromolecular assembly; \u0000Ntn hydrolases; \u0000PA28 activator","PeriodicalId":165163,"journal":{"name":"Biopolymers Online","volume":"32 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2002-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"131085701","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 : 2002-12-09DOI: 10.1002/3527600035.BPOL7002
M. Sisido
Introduction Historical Outline Extension of Amino Acids Chemical Aminoacylation Extension of Codons (Four-base Codons) Adaptability of Four-base Codons in the Ribosome System and Extension to Five-base Codons Nonnatural Base Pairs for Codon Extension In-vitro Protein Synthesis in the Presence of tRNAs that are Amino-acylated with Nonnatural Amino Acids Purification and Identification of Nonnatural Mutants Multiple Incorporation of Nonnatural amino acids by using Different Orthogonal Four-base Codons Mutants that Contain a Single Nonnatural Amino Acid at Random Positions Combination of In-vitro Synthesis and Chemical Synthesis for Screening Nonnatural Mutants and for Large-scale Production In-vivo Synthesis of Nonnatural Mutants Examples of Specialty Functions of Nonnatural Mutants Fluorescence Labeling Electron Transfers Inside Protein Frameworks Outlook and Perspectives Acknowledgments Keywords: nonnatural amino acids; chemical aminoacylation; codon extension; four-base codons; nonnatural base pairs; in-vitro protein synthesis; random insertion/deletion mutagenesis; fluorescence labeling; electron transfer
{"title":"Proteins Containing Nonnatural Amino Acids","authors":"M. Sisido","doi":"10.1002/3527600035.BPOL7002","DOIUrl":"https://doi.org/10.1002/3527600035.BPOL7002","url":null,"abstract":"Introduction \u0000Historical Outline \u0000Extension of Amino Acids \u0000Chemical Aminoacylation \u0000Extension of Codons (Four-base Codons) \u0000Adaptability of Four-base Codons in the Ribosome System and Extension to Five-base Codons \u0000Nonnatural Base Pairs for Codon Extension \u0000In-vitro Protein Synthesis in the Presence of tRNAs that are Amino-acylated with Nonnatural Amino Acids \u0000Purification and Identification of Nonnatural Mutants \u0000Multiple Incorporation of Nonnatural amino acids by using Different Orthogonal Four-base Codons \u0000Mutants that Contain a Single Nonnatural Amino Acid at Random Positions \u0000Combination of In-vitro Synthesis and Chemical Synthesis for Screening Nonnatural Mutants and for Large-scale Production \u0000In-vivo Synthesis of Nonnatural Mutants \u0000Examples of Specialty Functions of Nonnatural Mutants \u0000Fluorescence Labeling \u0000Electron Transfers Inside Protein Frameworks \u0000 \u0000 \u0000Outlook and Perspectives \u0000Acknowledgments \u0000 \u0000 \u0000Keywords: \u0000 \u0000nonnatural amino acids; \u0000chemical aminoacylation; \u0000codon extension; \u0000four-base codons; \u0000nonnatural base pairs; \u0000in-vitro protein synthesis; \u0000random insertion/deletion mutagenesis; \u0000fluorescence labeling; \u0000electron transfer","PeriodicalId":165163,"journal":{"name":"Biopolymers Online","volume":"45 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2002-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132240885","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 : 2002-12-09DOI: 10.1002/3527600035.BPOL7008
W. Wimley
Introduction Historical Outline The Fluid Mosaic Model of Biological Membranes Chemical Structures The Lipid Bilayer Milieu Physical Properties of Lipid Bilayer Membranes Polypeptides in Membranes Composition and Organization of Biological Membranes Genomics and Proteomics Biological Functions Information Transfer Material Transfer Transport Against Concentration Gradients Membrane Protein Enzymes Membrane Anchors Outlook and Perspectives Patents Keywords: bilayer; membrane; lipid; membrane protein; helical bundle; beta barrel; fluid mosaic; hydropathy
Pub Date : 2002-11-29DOI: 10.1002/3527600035.BPOL3A06
B. Rehm, A. Steinbüchel
Polyhydroxyalkanoic acids (PHAs) represent a rather complex class of polyesters that are synthesized by most genera of bacteria and members of the family Halobacteriaceae of the Archaea (Steinbuchel et al., 1997; Steinbuchel and Fuchtenbusch, 1998). Most of these prokaryotes synthesize poly(3-hydroxy-butyric acid), poly(3HB), and other PHAs as storage compounds and deposit these polyesters as insoluble inclusions in the cytoplasm. The number of 91 different constituents of PHAs that were recently compiled (Steinbuchel and Valentin, 1995) has meanwhile been outnumbered, and approximately 150 different hydroxyalkanoic acids are now known to occur as constituents of PHAs. These water-insoluble PHAs exhibit rather high molecular weights, thermoplastic and/or elastomeric features, and some other interesting physical and material properties. Therefore, and since they are biodegradable (Jendrossek et al., 1996), they are considered for several applications in the packaging industry, medicine, pharmacy, agriculture and food industry, or as raw materials for the synthesis of enantiomerically pure chemicals and the production of paints (Anderson and Dawes, 1990; Muller and Seebach, 1993; Hocking and Marchessault; 1994 Steinbuchel, 1996; Williams et al., 1999; van der Walle et al., 1999). Many prokaryotic and eukaryotic organisms are able to produce low-molecular weight poly(3HB) molecules that are complexed with other biomolecules and that occur at concentrations which are three to four orders of magnitude less than storage PHAs in the cells (Reusch and Sadoff, 1988). A few eukaryotic microorganisms such as for example Aureobasidium pullulans are able to synthesize the water-soluble polyester polymalic acid which is not synthesized by prokaryotes (Liu and Steinbuchel, 1996).
聚羟基烷酸(PHAs)是一类相当复杂的聚酯,由大多数细菌属和古细菌的盐杆菌科成员合成(Steinbuchel et al., 1997;Steinbuchel and Fuchtenbusch, 1998)。这些原核生物大多合成聚(3-羟基丁酸)、聚(3HB)和其他相芳烃作为储存化合物,并将这些聚酯作为不溶性包涵体沉积在细胞质中。最近汇编的PHAs的91种不同成分的数量(Steinbuchel和Valentin, 1995)同时也超过了数量,现在已知大约有150种不同的羟基烷酸作为PHAs的成分出现。这些不溶于水的pha具有相当高的分子量,热塑性和/或弹性体特征,以及一些其他有趣的物理和材料特性。因此,由于它们是可生物降解的(Jendrossek等人,1996),它们被认为在包装工业、医药、制药、农业和食品工业中有几种应用,或作为合成对映纯化学品和生产油漆的原料(Anderson和Dawes, 1990;Muller and Seebach, 1993;霍金与马尔切索;1994 Steinbuchel, 1996;Williams et al., 1999;van der Walle et al., 1999)。许多原核生物和真核生物能够产生低分子量的聚(3HB)分子,这些分子与其他生物分子络合,其浓度比细胞中储存的相has低三到四个数量级(Reusch和Sadoff, 1988)。一些真核微生物,如普鲁兰毛霉能够合成水溶性聚酯聚苹果酸,这是原核生物无法合成的(Liu and Steinbuchel, 1996)。
{"title":"Polyhydroxyalkanoate (PHA) Synthases: The Key Enzymes of PHA Synthesis","authors":"B. Rehm, A. Steinbüchel","doi":"10.1002/3527600035.BPOL3A06","DOIUrl":"https://doi.org/10.1002/3527600035.BPOL3A06","url":null,"abstract":"Polyhydroxyalkanoic acids (PHAs) represent a rather complex class of polyesters that are synthesized by most genera of bacteria and members of the family Halobacteriaceae of the Archaea (Steinbuchel et al., 1997; Steinbuchel and Fuchtenbusch, 1998). Most of these prokaryotes synthesize poly(3-hydroxy-butyric acid), poly(3HB), and other PHAs as storage compounds and deposit these polyesters as insoluble inclusions in the cytoplasm. The number of 91 different constituents of PHAs that were recently compiled (Steinbuchel and Valentin, 1995) has meanwhile been outnumbered, and approximately 150 different hydroxyalkanoic acids are now known to occur as constituents of PHAs. These water-insoluble PHAs exhibit rather high molecular weights, thermoplastic and/or elastomeric features, and some other interesting physical and material properties. Therefore, and since they are biodegradable (Jendrossek et al., 1996), they are considered for several applications in the packaging industry, medicine, pharmacy, agriculture and food industry, or as raw materials for the synthesis of enantiomerically pure chemicals and the production of paints (Anderson and Dawes, 1990; Muller and Seebach, 1993; Hocking and Marchessault; 1994 Steinbuchel, 1996; Williams et al., 1999; van der Walle et al., 1999). Many prokaryotic and eukaryotic organisms are able to produce low-molecular weight poly(3HB) molecules that are complexed with other biomolecules and that occur at concentrations which are three to four orders of magnitude less than storage PHAs in the cells (Reusch and Sadoff, 1988). A few eukaryotic microorganisms such as for example Aureobasidium pullulans are able to synthesize the water-soluble polyester polymalic acid which is not synthesized by prokaryotes (Liu and Steinbuchel, 1996).","PeriodicalId":165163,"journal":{"name":"Biopolymers Online","volume":"3 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2002-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"115527273","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 : 2002-11-29DOI: 10.1002/3527600035.BPOL3A05
R. Reusch
Introduction Historical Outline Complexes of cPHB with Inorganic Polyphosphates (cPHB/polyP) Protein-associated cPHAs Occurrence and Distribution of cPHAs Synthesis and Degradation of cPHAs Physical Properties of cPHAs Transbilayer Ion Transport by OHB Transbilayer Ion Transport by cPHB/polyP Complexes cPHB/polyP Complexes from E. coli in Planar Lipid Bilayers Synthetic Ion Channels from cPHB128 and PolyP Characteristics of cPHB/PolyP Ion Channels Structure of cPHB/PolyP Complexes Mechanism of cPHA/PolyP Channel Activity Putative Functions of cPHB/PolyP Complexes Protein-associated cPHAs Eubacteria Eukaryotes cPHA as Agents in Human Disease Atherosclerosis Diabetes Methods Isolation of cPHA Proteins Determination of cPHAs Evolutionary Aspects and Conclusions Outlook and Perspectives Keywords: complexed poly-(R)-3-hydroxyalkanoate; complexed poly-(R)-3-hydroxybutyrate; eukaryote; inorganic polyphosphate; poly-(R)-3-hydroxyalkanoate; poly-(R)-3-hydroxybutyrate; prokaryote
{"title":"Non‐Storage Poly‐(R)‐3‐hydroxyalkanoates (Complexed PHAs) in Prokaryotes and Eukaryotes","authors":"R. Reusch","doi":"10.1002/3527600035.BPOL3A05","DOIUrl":"https://doi.org/10.1002/3527600035.BPOL3A05","url":null,"abstract":"Introduction \u0000Historical Outline \u0000Complexes of cPHB with Inorganic Polyphosphates (cPHB/polyP) \u0000Protein-associated cPHAs \u0000 \u0000 \u0000Occurrence and Distribution of cPHAs \u0000Synthesis and Degradation of cPHAs \u0000Physical Properties of cPHAs \u0000Transbilayer Ion Transport by OHB \u0000Transbilayer Ion Transport by cPHB/polyP Complexes \u0000cPHB/polyP Complexes from E. coli in Planar Lipid Bilayers \u0000Synthetic Ion Channels from cPHB128 and PolyP \u0000Characteristics of cPHB/PolyP Ion Channels \u0000Structure of cPHB/PolyP Complexes \u0000Mechanism of cPHA/PolyP Channel Activity \u0000Putative Functions of cPHB/PolyP Complexes \u0000 \u0000 \u0000Protein-associated cPHAs \u0000Eubacteria \u0000Eukaryotes \u0000 \u0000 \u0000cPHA as Agents in Human Disease \u0000Atherosclerosis \u0000Diabetes \u0000 \u0000 \u0000Methods \u0000Isolation of cPHA Proteins \u0000Determination of cPHAs \u0000 \u0000 \u0000Evolutionary Aspects and Conclusions \u0000Outlook and Perspectives \u0000 \u0000 \u0000Keywords: \u0000 \u0000complexed poly-(R)-3-hydroxyalkanoate; \u0000complexed poly-(R)-3-hydroxybutyrate; \u0000eukaryote; \u0000inorganic polyphosphate; \u0000poly-(R)-3-hydroxyalkanoate; \u0000poly-(R)-3-hydroxybutyrate; \u0000prokaryote","PeriodicalId":165163,"journal":{"name":"Biopolymers Online","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2002-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"131563997","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}