Isolation of an altered form of DNA polymerase I from Escherichia coli cells induced for recA/lexA functions

Journal Article · Fri Jan 01 00:00:00 EST 1982 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.79.2.330· OSTI ID:5527712

Lackey, D; Krauss, S W; Linn, S

A novel form of DNA polymerase I (deoxynucleosidetriphosphate:DNA deoxynucleotidyltransferase, DNA nucleotidyltransferase, EC 2.7.7.7) activity has been isolated from Escherichia coli cells that had been activated for expression of the DNA damage-inducible genes. Induction was by treatment of normal cells or cells carrying the spr-51 and tif-1 mutations with nalidixic acid. This activity, DNA polymerase I*, seems to be a form of DNA polymerase I because it is insensitive to N-ethyllmaleimide, is inhibited by antibody to DNA polymerase I, and does not appear in a polA1 strain. DNA polymerase I* activity sediments through sucrose gradients as a broad peak with S/sub 20//sub ,w/ = 6.6-10.5, compared with an S/sub 20//sub,w/ = 4.8-5.5 for DNA polymerase I. The fidelity during polymerization reactions of DNA polymerase I* is relatively low with a variety of synthetic templates and deoxynucleosidetriphosphates, although the enzyme appears to have a normal level of 3'->5' exonuclease. Polymerase I* has properties that might implicate it in some form of mutagenic DNA repair.

• Research Organization: Univ. of California, Berkeley, CA (United States)
• OSTI ID: 5527712
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 79:2
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
POLYMERASES
CHEMICAL ACTIVATION
CHEMICAL ANALYSIS
BIOLOGICAL REPAIR
DNA
ENZYME ACTIVITY
ESCHERICHIA COLI
GENES
MUTAGENESIS
BACTERIA
BIOLOGICAL RECOVERY
ENZYMES
MICROORGANISMS
NUCLEIC ACIDS
NUCLEOTIDYLTRANSFERASES
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
RECOVERY
REPAIR
TRANSFERASES
550200* - Biochemistry