Pub Date : 2001-01-01DOI: 10.3109/10425170109084465
D. Jeoung, H. Kim
Ferritin serves as a storage protein for iron in animals. Complementary DNA encoding a heavy chain ferritin was cloned from the brain of Canis familiaris. The dog ferritin cDNA encodes a 182 amino acid that shows high levels of amino acid identity with vertebrate ferritins (90-98%). Near the cap region of the 5'-untranslated region, the dog H-ferritin mRNA displays a 28-nucleotide sequence that is exactly conserved in the corresponding region of the human and pig H-ferritin mRNA, thus making this sequence a prime candidate for involvement in the known translational regulation of H-ferritin by iron.
{"title":"Cloning and Sequence Analysis of cDNA for Heavy-chain Ferritin from the Canis familiaris","authors":"D. Jeoung, H. Kim","doi":"10.3109/10425170109084465","DOIUrl":"https://doi.org/10.3109/10425170109084465","url":null,"abstract":"Ferritin serves as a storage protein for iron in animals. Complementary DNA encoding a heavy chain ferritin was cloned from the brain of Canis familiaris. The dog ferritin cDNA encodes a 182 amino acid that shows high levels of amino acid identity with vertebrate ferritins (90-98%). Near the cap region of the 5'-untranslated region, the dog H-ferritin mRNA displays a 28-nucleotide sequence that is exactly conserved in the corresponding region of the human and pig H-ferritin mRNA, thus making this sequence a prime candidate for involvement in the known translational regulation of H-ferritin by iron.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"47 1","pages":"401 - 406"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82152050","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: 10.3109/10425170109080777
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: 10.3109/10425170109025000
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: 10.3109/10425170109025002
K. Adolph
Because of the close proximity of D. melanogaster gene CG11327 and the gene for a thrombospondin homologue (DTSP), the relationship between transcription of the two genes has been investigated. As part of this study, the cDNA sequence of gene CG11327 was determined, and structural features of the encoded protein were characterized. The CG11327 open reading frame specifies a polypeptide of 475 amino acid residues, molecular weight 53,666. The highly acidic protein has an aspartic acid+glutamic acid content of 23.2%. Weak similarities to other proteins suggest that it may function as a transcription factor or structural protein of the cell cycle. The existence of overlapping transcripts was found to be a significant feature of transcription of gene CG11327 and the DTSP gene. The 3′ end of the DTSP gene overlaps the 5′ end of gene CG11327 by at least 177 bp, and the region of overlap includes exon 13 and the 3′ UTR of the DTSP gene.
{"title":"Short Communication: Relationship of Transcription of Drosophila melanogaster Gene CG11327 and the Gene for a Thrombospondin Homologue (DTSP)","authors":"K. Adolph","doi":"10.3109/10425170109025002","DOIUrl":"https://doi.org/10.3109/10425170109025002","url":null,"abstract":"Because of the close proximity of D. melanogaster gene CG11327 and the gene for a thrombospondin homologue (DTSP), the relationship between transcription of the two genes has been investigated. As part of this study, the cDNA sequence of gene CG11327 was determined, and structural features of the encoded protein were characterized. The CG11327 open reading frame specifies a polypeptide of 475 amino acid residues, molecular weight 53,666. The highly acidic protein has an aspartic acid+glutamic acid content of 23.2%. Weak similarities to other proteins suggest that it may function as a transcription factor or structural protein of the cell cycle. The existence of overlapping transcripts was found to be a significant feature of transcription of gene CG11327 and the DTSP gene. The 3′ end of the DTSP gene overlaps the 5′ end of gene CG11327 by at least 177 bp, and the region of overlap includes exon 13 and the 3′ UTR of the DTSP gene.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"13 1","pages":"273 - 279"},"PeriodicalIF":0.0,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74782920","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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