Functional differences and regulation of gene expression of phosphoribosylpyrophophate synthetase isozymes
| Project/Area Number |
63570109
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Chiba University |
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Principal Investigator |
TAIRA Masanori Chiba University School of Medicine, Assistant, 医学部, 助手 (60150083)
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| Co-Investigator(Kenkyū-buntansha) |
TATIBANA Masamiti Chiba University School of Medicine Professor, 医学部, 教授 (50009081)
ISHIJIMA Sumio Chiba University School of Medicine, Assistant, 医学部, 助手 (70184520)
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| Project Period (FY) |
1988 – 1989
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| Project Status |
Completed (Fiscal Year 1989)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1989: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1988: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Phosphoribosylpyrophosphate / Phosphoribosylpyrophosphate synthetase / Isozyme / Gene expession / Chromosome mapping / cDNA sequence / Gene structure / Initiation codon / 組織特異的発現 / 精巣特異的発現 / ヌクレオチド合成 / cDNAクローニング / アイソフォーム / 組み換えDNA |
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| Research Abstract |
1. Cloning of CDNA coding rat phosphoribosylpyrophosphate synthetase revealed two distinct types of subunit, referred to as PRS I and PRS II. Tissue-specific expression of PRS I and PRS II genes was shown. In the testis, an additional transcript was noted.
2. The chromosomal localization of human PRS I and PRS II genes was determined. In addition, two PRPS1 (PRS I gene)-related genes (PRPS1L1 and PRPS1L2) were found.
3. Complete cDNA sequence of rat PRS I and PRS II were determined.
4. Genomic DNA corresponding to rat PRPS1 was cloned and characterized. The gene consisted of seven exons.
5. cDNA for testis-specific human phosphoribosylpyrophosphate synthetase was cloned and characterized. The gene was located at chromosome 7. The mRNA had a non-AUG initiation codon, ACG.
6. cDNAs for rat PRS I and PRS II were inserted into the vector and expressed in Escherichia coli. The enzyme activities of E. coli cells transformed with the expression vectors were 10-20 fold greater than that of untransformed E. coli cells.
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Report
(3 results)
Research Products
(18 results)
