NDLI: A unique deoxyguanosine triphosphatase is responsible for the optA1 phenotype of Escherichia coli.

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A unique deoxyguanosine triphosphatase is responsible for the optA1 phenotype of Escherichia coli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Beauchamp, B. B. Richardson, C. C.
Description	Author Affiliation: Beauchamp BB ( Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.);
Abstract	Escherichia coli optA1, a mutant unable to support the growth of T7 phage containing mutations in gene 1.2, contains reduced amounts of dGTP. Extracts of E. coli optA1 catalyze the hydrolysis of dGTP at a rate 50-fold greater than do extracts of E. coli optA+. The dGTPase responsible for the increased hydrolysis has been purified to apparent homogeneity. Purification of the protein is facilitated by its high affinity for single-stranded DNA. By using this purification scheme an identical dGTPase has been purified from E. coli optA+. The purified proteins catalyze the hydrolysis of dGTP to yield deoxyguanosine and tripolyphosphate. The products of hydrolysis, chromatographic properties, denatured molecular mass of 56 kDa, N-terminal amino acid sequence, substrate specificity, and heat inactivation indicate that the proteins purified from optA1 and from optA+ cells are identical and identify the enzyme as the deoxyguanosine 5'-triphosphate triphosphohydrolase purified to homogeneity from wild-type E. coli [Seto, D., Bhatnagar, S. K. & Bessman, M. J. (1988) J. Biol. Chem. 263, 1494-1499]. OptA1 cells contain approximately equal to 50-fold more active molecules of the 56-kDa dGTPase than do E. coli optA+ cells.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	8
Volume Number	85
Language	English
Publisher	National Academy of Sciences
Publisher Date	1988-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Deoxyguanine Nucleotides Metabolism Escherichia Coli Genetics Phosphoric Monoester Hydrolases Physiology T-Phages Growth & Development Enzymology Genes, Bacterial Hot Temperature Kinetics Molecular Weight Mutation Isolation & Purification Substrate Specificity Virus Replication Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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