Pyridoxal 5'-phosphate mediated inactivation of Escherichia coli DNA polymerase I: identification of lysine-635 as an essential residue for the processive mode of DNA synthesis

Journal Article · Tue Sep 06 04:00:00 EDT 1988 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00418a011· OSTI ID:6518147

Basu, S; Basu, A; Modak, M J

Inactivation of Escherichia coli DNA polymerase I by pyridoxal 5'-phosphate treatment results from its reactivity at multiple lysine residues. One of these residues, lysine-758, has been shown to be located at the substrate binding site in DNA polymerase I. We now demonstrate that lysine-635 is another important target of pyridoxylation; modification of this site results in decreased rates of DNA synthesis. Addition of template-primer with or without substrate deoxynucleoside triphosphate protects lysine-635 from pyridoxylation. Analysis of the initiation versus elongation phase of DNA synthesis by lysine-635-modified enzyme revealed that elongation of the DNA chain is severely affected by the lysine-635 modification. We therefore conclude that this lysine residue plays an important role in the processive mode of DNA synthesis by E. coli DNA polymerase I.

• Research Organization: Univ. of Medicine and Dentistry, Newark, NJ (USA)
• OSTI ID: 6518147
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:18; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
BACTERIA
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL FUNCTIONS
BIOLOGICAL RECOVERY
BIOLOGICAL REPAIR
CARBOXYLIC ACIDS
DNA POLYMERASES
DNA REPAIR
ENZYMES
ESCHERICHIA COLI
FUNCTIONS
HYDROLASES
KINETICS
LYSINE
MEMBRANE PROTEINS
MICROORGANISMS
NUCLEOTIDYLTRANSFERASES
ORGANIC ACIDS
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PHOSPHORUS-GROUP TRANSFERASES
POLYMERASES
PROTEINS
REACTION KINETICS
RECEPTORS
RECOVERY
REPAIR
SERINE PROTEINASES
TRANSFERASES
TRYPSIN