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| HUMAN GMP SYNTHETASE - PROTEIN-PURIFICATION, CLONING, AND FUNCTIONAL EXPRESSION OF CDNA |
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| Author(s): HIRST M, HALIDAY E, NAKAMURA J, LOU L |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 269 Issue: 38 Pages: 23830-23837 Published: SEP 23 1994 |
| Times Cited: 19 References: 51 |
| Abstract: (i)GMP synthetase is a key enzyme in the de novo synthesis of guanine nucleotides. Human GRIP synthetase has been purified to homogeneity, and a cDNA encoding the enzyme has been isolated from the T-lymphoblastoma cell line, A3.01. The open reading frame encodes a protein of 693 amino acids with a predicted molecular weight of 76,725. The cDNA complements a guaA mutant of Escherichia coli, which lacks a functional GRIP synthetase and extracts from the transformed E. coli exhibit GMP synthetase activity, which is absent in the parental strain. RNA hybridization analysis shows that human GRIP synthetase is encoded by a single 2.4-kilobase message, DNA hybridization analysis suggests that the human GMP synthetase is encoded by one gene. In several human cell lines, the level of mRNA expression is substantially higher in proliferating, transformed cells than in nontransformed cells. In two transformed cell lines, treatment with phorbol ester inhibits proliferation and results in a dramatic down-regulation in the levels of GMP synthetase mRNA and protein. |
| Document Type: Article |
| Language: English |
Addresses:
1. SYNTEX INC, DISCOVERY RES, INST BIOCHEM & CELL BIOL, PALO ALTO, CA 94303 USA |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: PQ345 |
| ISSN: 0021-9258 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |