DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, YS | - |
dc.contributor.author | Nosaka, K | - |
dc.contributor.author | Downs, DM | - |
dc.contributor.author | Kwak, JM | - |
dc.contributor.author | Park, D | - |
dc.contributor.author | Chung, IK | - |
dc.contributor.author | Nam, HG | - |
dc.date.accessioned | 2016-03-31T13:51:12Z | - |
dc.date.available | 2016-03-31T13:51:12Z | - |
dc.date.created | 2009-03-20 | - |
dc.date.issued | 1998-08 | - |
dc.identifier.issn | 0167-4412 | - |
dc.identifier.other | 1998-OAK-0000000327 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/20704 | - |
dc.description.abstract | We report the characterization of a Brassica napus cDNA clone (pBTH1) encoding a protein (BTH1) with two enzymatic activities in the thiamin biosynthetic pathway, thiamin-phosphate pyrophosphorylase (TMP-PPase) and 2-methyl-4-amino-5-hydroxymethylpyrimidine-monophosphate kinase (HMP-P kinase). The cDNA clone was isolated by a novel functional complementation strategy employing an Escherichia coli mutant deficient in the TMP-PPase activity. A biochemical assay showed the clone to confer recovery of TMP-PPase activity in the E. coli mutant strain. The cDNA clone is 1746 bp long and contains an open reading frame encoding a peptide of 524 amino acids. The C-terminal part of BTH1 showed 53% and 59% sequence similarity to the N-terminal TMP-PPase region of the bifunctional yeast proteins Saccharomyces THI6 and Schizosaccharomyces pombe THI4, respectively. The N-terminal part of BTH1 showed 58% sequence similarity to HMP-P kinase of Salmonella typhimurium. The cDNA clone functionally complemented the S. typhimurium and E. coli thiD mutants deficient in the HMP-P kinase activity. These results show that the clone encodes a bifunctional protein with TMP-PPase at the C-terminus and HMP-P kinase at the N-terminus. This is in contrast to the yeast bifunctional proteins that encode TMP-PPase at the N-terminus and 4-methyl-5-(2-hydroxyethyl)thiazole kinase at the C-terminus, Expression of the BTH1 gene is negatively regulated by thiamin, as in the cases for the thiamin biosynthetic genes of microorganisms. This is the first report of a plant thiamin biosynthetic gene on which a specific biochemical activity is assigned. The Brassica BTH1 gene may correspond to the Arabidopsis TH-1 gene. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | KLUWER ACADEMIC PUBL | - |
dc.relation.isPartOf | PLANT MOLECULAR BIOLOGY | - |
dc.subject | bifunctional enzyme | - |
dc.subject | Brassica napus | - |
dc.subject | cDNA | - |
dc.subject | hydroxymethylpyrimidine phosphate kinase | - |
dc.subject | thiamin | - |
dc.subject | thiamin phosphate pyrophosphorylase | - |
dc.subject | REDUCTASE-THYMIDYLATE SYNTHASE | - |
dc.subject | ARABIDOPSIS-THALIANA | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | SACCHAROMYCES-CEREVISIAE | - |
dc.subject | FUNCTIONAL COMPLEMENTATION | - |
dc.subject | HYDROXYETHYLTHIAZOLE KINASE | - |
dc.subject | PISUM-SATIVUM | - |
dc.subject | GENE | - |
dc.subject | ALIGNMENT | - |
dc.subject | SEQUENCES | - |
dc.title | A Brassica cDNA clone encoding a bifunctional hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase involved in thiamin biosynthesis | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1023/A:1006030617502 | - |
dc.author.google | Kim, YS | - |
dc.author.google | Nosaka, K | - |
dc.author.google | Downs, DM | - |
dc.author.google | Kwak, JM | - |
dc.author.google | Park, D | - |
dc.author.google | Chung, IK | - |
dc.author.google | Nam, HG | - |
dc.relation.volume | 37 | - |
dc.relation.issue | 6 | - |
dc.relation.startpage | 955 | - |
dc.relation.lastpage | 966 | - |
dc.contributor.id | 10087591 | - |
dc.relation.journal | PLANT MOLECULAR BIOLOGY | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | PLANT MOLECULAR BIOLOGY, v.37, no.6, pp.955 - 966 | - |
dc.identifier.wosid | 000075075800006 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 966 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 955 | - |
dc.citation.title | PLANT MOLECULAR BIOLOGY | - |
dc.citation.volume | 37 | - |
dc.contributor.affiliatedAuthor | Nam, HG | - |
dc.identifier.scopusid | 2-s2.0-0345395999 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 26 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | REDUCTASE-THYMIDYLATE SYNTHASE | - |
dc.subject.keywordPlus | ARABIDOPSIS-THALIANA | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | FUNCTIONAL COMPLEMENTATION | - |
dc.subject.keywordPlus | HYDROXYETHYLTHIAZOLE KINASE | - |
dc.subject.keywordPlus | PISUM-SATIVUM | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | ALIGNMENT | - |
dc.subject.keywordPlus | SEQUENCES | - |
dc.subject.keywordAuthor | bifunctional enzyme | - |
dc.subject.keywordAuthor | Brassica napus | - |
dc.subject.keywordAuthor | cDNA | - |
dc.subject.keywordAuthor | hydroxymethylpyrimidine phosphate kinase | - |
dc.subject.keywordAuthor | thiamin | - |
dc.subject.keywordAuthor | thiamin phosphate pyrophosphorylase | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Plant Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Plant Sciences | - |
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