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PMID: 6153063 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Base excision repair in the thermophile Thermus sp. strain X-1.

Journal of bacteriology ·Vol. 154 ·No. 3 ·1983-06-00 ·Pages 1451-4

Warner HR

Abstract

The thermophile Thermus sp. strain X-1, grown at 70 degrees C, contains uracil-DNA glycosylase and apurinic endonuclease activities, both of which are known to have roles in the repair of DNA damaged by heat. Both of these activities have temperature optima of about 70 degrees C. However, neither of these activities is present in quantities significantly greater than that found in Escherichia coli grown at 37 degrees C. Therefore, it appears that thermophilic organisms may not contain greatly elevated levels of the enzymes thought to be involved in the repair of DNA damaged by heat.

MeSH Terms
DNA Glycosylases DNA Repair DNA, Bacterial/metabolism DNA-(Apurinic or Apyrimidinic Site) Lyase Deoxyribonuclease IV (Phage T4-Induced) Endodeoxyribonucleases/metabolism Escherichia coli Proteins Hot Temperature N-Glycosyl Hydrolases/metabolism Thermus/enzymology,metabolism Uracil-DNA Glycosidase
Chemicals
DNA, Bacterial Escherichia coli Proteins Endodeoxyribonucleases Deoxyribonuclease IV (Phage T4-Induced) endonuclease IV, E coli DNA Glycosylases N-Glycosyl Hydrolases Uracil-DNA Glycosidase DNA-(Apurinic or Apyrimidinic Site) Lyase
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Warner H R
References (14)
14 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1983-06-00
Pages
1451-4
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC217623
Subset
IM
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