Pub Date : 2001-01-01DOI: 10.3109/10425170109080777
Sung Joong Lee, Kathryn Drabik, E. Benveniste
Rat calcium-modulating cyclophilin ligand (CAML) cDNA was cloned and sequenced. It has a predicted open reading frame of 294 amino acids. The CAML gene is highly conserved throughout species, showing 85, 89 and 69% amino acid sequence identity to the human, mouse, and chicken genes, respectively. Gene expression data using astrocytes, microglia and neurons show that CAML mRNA and protein is constitu-tively expressed in these cell types of the central nervous system. The cloning of rat CAML will facilitate further investigations on the function of this molecule.
{"title":"Cloning of Rat Calcium-Modulating Cyclophilin Ligand","authors":"Sung Joong Lee, Kathryn Drabik, E. Benveniste","doi":"10.3109/10425170109080777","DOIUrl":"https://doi.org/10.3109/10425170109080777","url":null,"abstract":"Rat calcium-modulating cyclophilin ligand (CAML) cDNA was cloned and sequenced. It has a predicted open reading frame of 294 amino acids. The CAML gene is highly conserved throughout species, showing 85, 89 and 69% amino acid sequence identity to the human, mouse, and chicken genes, respectively. Gene expression data using astrocytes, microglia and neurons show that CAML mRNA and protein is constitu-tively expressed in these cell types of the central nervous system. The cloning of rat CAML will facilitate further investigations on the function of this molecule.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"88 1","pages":"209 - 213"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88230761","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 : 2001-01-01DOI: 10.3109/10425170109042054
F. Alarcón-Chaidez, C. Bender
s`54, which is encoded by rpoN, is required for a variety of metabolic functions in bacteria including the utilization of alternative carbon and nitrogen sources, nitrogen fixation, and the expression of virulence determinants. Sequence analysis of a 3, 020-bp DNA fragment from the plant pathogen Pseudomonas syringae pv. glycinea PG4180 revealed four ORFs designated rpoN, orfA, orfB, and orfCδ, which were related to rpoN and rpoN-associated genes from other microorganisms. The rpoN upstream region in P. syringae contained two overlapping promoters, which may suggest a complex regulatory pattern. This is the first study describing the organization of the rpoN locus in P. syringae.
{"title":"Analysis of the rpoN Locus in the Plant Pathogenic Bacterium, Pseudomonas Syringae pv. Glycinea","authors":"F. Alarcón-Chaidez, C. Bender","doi":"10.3109/10425170109042054","DOIUrl":"https://doi.org/10.3109/10425170109042054","url":null,"abstract":"s`54, which is encoded by rpoN, is required for a variety of metabolic functions in bacteria including the utilization of alternative carbon and nitrogen sources, nitrogen fixation, and the expression of virulence determinants. Sequence analysis of a 3, 020-bp DNA fragment from the plant pathogen Pseudomonas syringae pv. glycinea PG4180 revealed four ORFs designated rpoN, orfA, orfB, and orfCδ, which were related to rpoN and rpoN-associated genes from other microorganisms. The rpoN upstream region in P. syringae contained two overlapping promoters, which may suggest a complex regulatory pattern. This is the first study describing the organization of the rpoN locus in P. syringae.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"88 1","pages":"77 - 84"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83811720","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 : 2001-01-01DOI: 10.3109/10425170109042046
A. Mazur, Jarostaw E. Król, A. Skorupska
Rhizobium leguminosarum bv. trifolii produces an acidic exopolysaccharide (EPS) that plays an important role in symbiotic interaction with clover plants. The sequence of 6.0-kb DNA fragment located upstream of the previously described prsDEorf3 and pssCDE genes involved in exopolysaccharide biosynthesis revealed three new genes designated pssN, pssO and pssP. The predicted protein product of pssP gene shares a significant homology to members of the membrane-peri-plasmic auxiliary (MPA1) family, that are involved in polymerization of the repeating subunits of EPS. The putative pssN protein product is highly homologous to the family of the outer membrane auxiliary (OMA) proteins engaged in translocation of polysaccharides in bacteria. The PssO did not reveal homology to the known bacterial proteins, but showed characteristic features of outer membrane proteins, and with PssN and PssP, it might be a part of the system involved in polymerization and translocation of EPS across the bacterial membranes.
{"title":"Isolation and Sequencing of Rhizobium Leguminosarum Bv. Trifolii PssN, PssO and PssP Genes Encoding the Proteins Involved in Polymerization and Translocation of Exopolysaccharide","authors":"A. Mazur, Jarostaw E. Król, A. Skorupska","doi":"10.3109/10425170109042046","DOIUrl":"https://doi.org/10.3109/10425170109042046","url":null,"abstract":"Rhizobium leguminosarum bv. trifolii produces an acidic exopolysaccharide (EPS) that plays an important role in symbiotic interaction with clover plants. The sequence of 6.0-kb DNA fragment located upstream of the previously described prsDEorf3 and pssCDE genes involved in exopolysaccharide biosynthesis revealed three new genes designated pssN, pssO and pssP. The predicted protein product of pssP gene shares a significant homology to members of the membrane-peri-plasmic auxiliary (MPA1) family, that are involved in polymerization of the repeating subunits of EPS. The putative pssN protein product is highly homologous to the family of the outer membrane auxiliary (OMA) proteins engaged in translocation of polysaccharides in bacteria. The PssO did not reveal homology to the known bacterial proteins, but showed characteristic features of outer membrane proteins, and with PssN and PssP, it might be a part of the system involved in polymerization and translocation of EPS across the bacterial membranes.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"1 1","pages":"1 - 12"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89401906","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 : 2001-01-01DOI: 10.3109/10425170109084469
Otor Al-Khalilt, B. Duke, S. Zeltwanger, D. Eaton, B. Spier, J. Stockand
The cellular homolog of the oncogene v-src, the proto-oncogene c-src, was cloned from rat testis using a high stringency polymerase chain reaction. Rat c-src cDNA shared identity with chicken and mouse, and Rous sarcoma virus c-src and v-src, respectively. Rat c-Src protein was 98% homologous to both human and mouse c-Src. Interestingly, rat Src contained one extra amino acid compared to the mouse protein. As expected, the rat testis Src lacked the six extra residues common to the neuronal Src identified in human and mouse. Reporting of the cDNA sequence for non-neuronal, rat c-src should facilitate experimentation into cell growth and transformation using rat tissues as models of human disease.
{"title":"Cloning of the Proto-oncogene c-src from Rat Testis","authors":"Otor Al-Khalilt, B. Duke, S. Zeltwanger, D. Eaton, B. Spier, J. Stockand","doi":"10.3109/10425170109084469","DOIUrl":"https://doi.org/10.3109/10425170109084469","url":null,"abstract":"The cellular homolog of the oncogene v-src, the proto-oncogene c-src, was cloned from rat testis using a high stringency polymerase chain reaction. Rat c-src cDNA shared identity with chicken and mouse, and Rous sarcoma virus c-src and v-src, respectively. Rat c-Src protein was 98% homologous to both human and mouse c-Src. Interestingly, rat Src contained one extra amino acid compared to the mouse protein. As expected, the rat testis Src lacked the six extra residues common to the neuronal Src identified in human and mouse. Reporting of the cDNA sequence for non-neuronal, rat c-src should facilitate experimentation into cell growth and transformation using rat tissues as models of human disease.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"80 1","pages":"425 - 429"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75618768","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 : 2001-01-01DOI: 10.3109/10425170109025000
T. Sjakste, N. Sjakste, K. Scherrer
The exon/intron structure of the human proteasome PROS-27 gene was established by means of partial sequencing of its genomic clones and comparison with the chromosome 14 sequences from the data bases. The gene contains seven exons spanning over 19 kb. Introns of the gene contain numerous Alu type repeats, Mer 2 and LINE type repeats. Pattern of the repeats indicates conservatism of the sequence.
{"title":"Short Communication: Exon/Intron Organisation of Human Proteasome PROS-27 K Gene","authors":"T. Sjakste, N. Sjakste, K. Scherrer","doi":"10.3109/10425170109025000","DOIUrl":"https://doi.org/10.3109/10425170109025000","url":null,"abstract":"The exon/intron structure of the human proteasome PROS-27 gene was established by means of partial sequencing of its genomic clones and comparison with the chromosome 14 sequences from the data bases. The gene contains seven exons spanning over 19 kb. Introns of the gene contain numerous Alu type repeats, Mer 2 and LINE type repeats. Pattern of the repeats indicates conservatism of the sequence.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"12 1","pages":"261 - 265"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81834218","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 : 2001-01-01DOI: 10.3109/10425170109084461
H. Tan, R. G. Creech, J. Jenkins, Yungfu Chang, D. Ma
Two cotton (Gossypium hirsutum L.) genes, ghprpl and ghprpl, encoding cell wall proline-rich proteins (PRPs) have been cloned and characterized. The ghprpl gene has an open reading frame (ORF) that encodes a PRP of 299 amino acids (aa), whereas the ghprp2 gene contains an ORF that codes for a 310-aa PRP. The GhPRPl has an 80% identity in aa sequence with that of GhPRP2. Like other plant cell wall PRPs, both cotton PRPs have a hydrophobic signal peptide at their N-termini, followed by repeating peptide units. Northern blot analyses showed that the ghprp1 gene is predominantly expressed in the fiber during the elongation stage of fiber development. Reverse transcription (RT)-PCR analysis showed that ghprp1 is expressed in both fiber and root tissues, whereas ghprpl is in roots only. The ghprp1 gene was shown to be present in the A1, A2, D1 and D5 genomes of Gossypium by PCR amplification, whereas the ghprpl gene is only present in the A1 and A2 genomes. The ghprp1 gene was over-expressed in the yeast Pichia pastoris, and the expressed GhPRP1 protein was used as an antigen to raise polyclonal antibodies (anti-GhPRP1). Western analysis using the anti-GhPRP1 probe detected a major protein band (50 kDa) in 5-31-day postanthesis (DPA) fibers. However, the 50 kDa protein was absent in other cotton tissues.
{"title":"Cloning and Expression Analysis of Two Cotton (Gossypium Hirsutum L.) Genes Encoding Cell Wall Proline-rich Proteins","authors":"H. Tan, R. G. Creech, J. Jenkins, Yungfu Chang, D. Ma","doi":"10.3109/10425170109084461","DOIUrl":"https://doi.org/10.3109/10425170109084461","url":null,"abstract":"Two cotton (Gossypium hirsutum L.) genes, ghprpl and ghprpl, encoding cell wall proline-rich proteins (PRPs) have been cloned and characterized. The ghprpl gene has an open reading frame (ORF) that encodes a PRP of 299 amino acids (aa), whereas the ghprp2 gene contains an ORF that codes for a 310-aa PRP. The GhPRPl has an 80% identity in aa sequence with that of GhPRP2. Like other plant cell wall PRPs, both cotton PRPs have a hydrophobic signal peptide at their N-termini, followed by repeating peptide units. Northern blot analyses showed that the ghprp1 gene is predominantly expressed in the fiber during the elongation stage of fiber development. Reverse transcription (RT)-PCR analysis showed that ghprp1 is expressed in both fiber and root tissues, whereas ghprpl is in roots only. The ghprp1 gene was shown to be present in the A1, A2, D1 and D5 genomes of Gossypium by PCR amplification, whereas the ghprpl gene is only present in the A1 and A2 genomes. The ghprp1 gene was over-expressed in the yeast Pichia pastoris, and the expressed GhPRP1 protein was used as an antigen to raise polyclonal antibodies (anti-GhPRP1). Western analysis using the anti-GhPRP1 probe detected a major protein band (50 kDa) in 5-31-day postanthesis (DPA) fibers. However, the 50 kDa protein was absent in other cotton tissues.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"22 1","pages":"367 - 380"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89359590","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 : 2001-01-01DOI: 10.3109/10425170109080774
Diane Rees, M. J. Fisher, I. McDowall
We have characterized the 5′-end (3218bp) of the rat phenylalanine hydroxylase (PAH) gene. Within this PAH promoter sequence, we have identified a number of putative regulatory sites analogous to those present in the human and murine PAH promoters. In particular, potential HNF 1 binding sites and a CRE have been identified. These sequences respectively bind HNF1 and CREB transcription factors present in rat nuclear extracts and may be significant in the tissue-specific and hormonal control of PAH expression.
{"title":"Sequence Analysis of the Rat Phenylalanine Hydroxylase Gene Promoter","authors":"Diane Rees, M. J. Fisher, I. McDowall","doi":"10.3109/10425170109080774","DOIUrl":"https://doi.org/10.3109/10425170109080774","url":null,"abstract":"We have characterized the 5′-end (3218bp) of the rat phenylalanine hydroxylase (PAH) gene. Within this PAH promoter sequence, we have identified a number of putative regulatory sites analogous to those present in the human and murine PAH promoters. In particular, potential HNF 1 binding sites and a CRE have been identified. These sequences respectively bind HNF1 and CREB transcription factors present in rat nuclear extracts and may be significant in the tissue-specific and hormonal control of PAH expression.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"1 1","pages":"191 - 195"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86543084","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 : 2001-01-01DOI: 10.3109/10425170109042047
Sabine Bernauer, M. Wehling, Dirk Gerdes And, E. Falkenstein
Rapid, nongenomic effects of steroids are likely to be mediated by membrane receptors not by intracellular steroid receptors. We recently identified a progesterone membrane binding protein (mPR) from human liver. The corresponding hmpr gene is comprised of 3 exons and 2 introns. The promoter sequence of hmpr lacks a typical TATA box but contains instead a high homology to a transcription Initiatior consensus sequence, which overlaps the experimentally determined transcriptional start site. The major proximal promoter is GC-rich and sequence analysis revealed a CpG island spanning the transcriptional start site. Several putative cis-regulatory DNA-motifs, which represent possible binding sites for transcription factors like AP2, NF-AT, Ahr/Arnt and C/EBP were identified in the genomic upstream region by sequence homology. Functional analysis of differently deleted fragments of the hmpr upstream region in a GFP-reportergene assay in transiently transfected cultured cells indicates the general testability of the hmpr promoter in vivo.
{"title":"The Human Membrane Progesterone Receptor Gene: Genomic Structure and Promoter Analysis","authors":"Sabine Bernauer, M. Wehling, Dirk Gerdes And, E. Falkenstein","doi":"10.3109/10425170109042047","DOIUrl":"https://doi.org/10.3109/10425170109042047","url":null,"abstract":"Rapid, nongenomic effects of steroids are likely to be mediated by membrane receptors not by intracellular steroid receptors. We recently identified a progesterone membrane binding protein (mPR) from human liver. The corresponding hmpr gene is comprised of 3 exons and 2 introns. The promoter sequence of hmpr lacks a typical TATA box but contains instead a high homology to a transcription Initiatior consensus sequence, which overlaps the experimentally determined transcriptional start site. The major proximal promoter is GC-rich and sequence analysis revealed a CpG island spanning the transcriptional start site. Several putative cis-regulatory DNA-motifs, which represent possible binding sites for transcription factors like AP2, NF-AT, Ahr/Arnt and C/EBP were identified in the genomic upstream region by sequence homology. Functional analysis of differently deleted fragments of the hmpr upstream region in a GFP-reportergene assay in transiently transfected cultured cells indicates the general testability of the hmpr promoter in vivo.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"111 1","pages":"13 - 25"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85795293","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 : 2001-01-01DOI: 10.3109/10425170109080775
B. Blitvich, A. Rayms-keller, C. Blair, B. Beaty
Many insects survive adverse climatic conditions in a dormant state known as diapause. In this study, we identified and sequenced several mRNAs in diapausing Aedes triseriatus mosquito embryos. Using reverse-transcription PCR and 5′ RACE, we identified a 995-nucleotide cDNA that encodes a 259-amino acid protein of unknown function. This putative protein displays strong sequence similarity to Drosophila mela-nogaster (95%), human (87%), Caenorhabditis elegans (86%) and yeast (81%) counterparts. The second identified full-length cDNA consists of 624 nucleotides and encodes a 174-amino acid protein of unknown function. This putative protein displays significant sequence similarity to D. melanogaster (68%), human (59%), plant (57%) and yeast (49%) counterparts. We also detected a number of cDNA fragments that exhibited significant sequence similarity to a mitochondrial cytochrome C oxidase subunit, human N33 protein (a potential human prostate tumor suppressor), 18S and 28S ribosomal RNAs, protein disulfide-isomerase, and guanine nucleotide-binding protein.
{"title":"Identification and Sequence Determination of mRNAs Detected in Dormant (Diapausing) Aedes triseriatus Mosquito Embryos","authors":"B. Blitvich, A. Rayms-keller, C. Blair, B. Beaty","doi":"10.3109/10425170109080775","DOIUrl":"https://doi.org/10.3109/10425170109080775","url":null,"abstract":"Many insects survive adverse climatic conditions in a dormant state known as diapause. In this study, we identified and sequenced several mRNAs in diapausing Aedes triseriatus mosquito embryos. Using reverse-transcription PCR and 5′ RACE, we identified a 995-nucleotide cDNA that encodes a 259-amino acid protein of unknown function. This putative protein displays strong sequence similarity to Drosophila mela-nogaster (95%), human (87%), Caenorhabditis elegans (86%) and yeast (81%) counterparts. The second identified full-length cDNA consists of 624 nucleotides and encodes a 174-amino acid protein of unknown function. This putative protein displays significant sequence similarity to D. melanogaster (68%), human (59%), plant (57%) and yeast (49%) counterparts. We also detected a number of cDNA fragments that exhibited significant sequence similarity to a mitochondrial cytochrome C oxidase subunit, human N33 protein (a potential human prostate tumor suppressor), 18S and 28S ribosomal RNAs, protein disulfide-isomerase, and guanine nucleotide-binding protein.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"54 1","pages":"197 - 202"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73526789","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 : 2001-01-01DOI: 10.3109/10425170109041333
D. Panetta, L. Yin, R. Barale, G. Romeo, R. Ravazzolo, Isabella Ceccherinp, A. Pulit
The RET proto-oncogene is involved in the development of both kidney and neural crests derived tissues. RET deleterious mutations cause hereditary neuroendocrine tumours and congenital intestinal agangliono-sis. Ongoing efforts aimed at elucidating the function of this gene include expression studies in different species and in transgenic mice. As first step in the study of Ret expression in mouse, we obtained the mouse Ret genomic structure. Intron-exon boundaries were determined and sequenced, all introns but the first one were amplified and cloned, and exons positioned in a restriction map. Mouse and human genes comparison indicates a highly conserved genomic organisation, except for exon 21 which is not conserved in mouse. A region extending 386 bp 5′ to the first exon was sequenced and compared with its human counterpart. Some features, reported for the human promoter, like the absence of TATA or CAAT boxes and a high GC content, are conserved.
RET原癌基因参与肾脏和神经嵴衍生组织的发育。RET有害突变可引起遗传性神经内分泌肿瘤和先天性肠神经节病。正在进行的旨在阐明该基因功能的工作包括在不同物种和转基因小鼠中的表达研究。作为小鼠Ret表达研究的第一步，我们获得了小鼠Ret基因组结构。确定内含子和外显子的边界并测序，扩增和克隆除第一个内含子外的所有内含子，并将外显子定位在限制子图中。小鼠与人类基因比较表明，除外显子21在小鼠中不保守外，其他基因组组织高度保守。测序了一个延伸至第一个外显子386 bp 5 '的区域，并与人类的对应区域进行了比较。据报道，人类启动子的一些特征，如没有TATA或CAAT盒和高GC含量，是保守的。
{"title":"Genomic Organisation of the Mouse Ret Proto-Oncogene","authors":"D. Panetta, L. Yin, R. Barale, G. Romeo, R. Ravazzolo, Isabella Ceccherinp, A. Pulit","doi":"10.3109/10425170109041333","DOIUrl":"https://doi.org/10.3109/10425170109041333","url":null,"abstract":"The RET proto-oncogene is involved in the development of both kidney and neural crests derived tissues. RET deleterious mutations cause hereditary neuroendocrine tumours and congenital intestinal agangliono-sis. Ongoing efforts aimed at elucidating the function of this gene include expression studies in different species and in transgenic mice. As first step in the study of Ret expression in mouse, we obtained the mouse Ret genomic structure. Intron-exon boundaries were determined and sequenced, all introns but the first one were amplified and cloned, and exons positioned in a restriction map. Mouse and human genes comparison indicates a highly conserved genomic organisation, except for exon 21 which is not conserved in mouse. A region extending 386 bp 5′ to the first exon was sequenced and compared with its human counterpart. Some features, reported for the human promoter, like the absence of TATA or CAAT boxes and a high GC content, are conserved.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"69 1","pages":"501 - 506"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89105071","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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