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[The effect of SSB-protein from Ehrlich ascites carcinoma cells on activity of various enzymes of DNA replication and repair].

Abstract
The effect of a single-stranded DNA-binding protein (SSB-protein) form Ehrlich ascites tumour cells (EAT) on the activity of homologous purified DNA-polymerases alpha and beta, DNA-replicase, primase and DNA-polymerases from phage T4 and Bacillus stearothermophillus was studied. It was shown that the SSB-protein caused a 1.5-2.5-fold stimulation of the DNA-polymerase alpha activity on different templates (e.g., denaturated and activated DNA, poly(dA). The degree of stimulation depended on the template type, protein/template ratio and purity of DNA-polymerase alpha. The activity of DNA-polymerase was inhibited by the SSB-protein, when the activated DNA was used as a matrix and was unchanged on the denaturated DNA. The activity of some prokaryotic DNA-polymerases was increased under the influence of the SSB-protein. The protein enhanced the processivity of T4 DNA-polymerase and strongly inhibited the activity of replicase and primase. A conclusion about the complex effect of the SSB-protein on the activity of replicative and repair enzymes is drawn.
AuthorsA N Koterov, N A Novoradovskaia, I V Filippovich
JournalBiokhimiia (Moscow, Russia) (Biokhimiia) Vol. 53 Issue 8 Pg. 1278-87 (Aug 1988) ISSN: 0320-9725 [Print] Russia (Federation)
Vernacular TitleVliianie SSB-belka iz kletok astsitnoĭ kartsinomy Erlikha na aktivnost' nekotorykh fermentov replikatsii i reparatsii DNK.
PMID3191193 (Publication Type: Journal Article)
Chemical References
  • DNA-Binding Proteins
  • Neoplasm Proteins
  • DNA Polymerase I
  • DNA Polymerase II
Topics
  • Animals
  • Carcinoma, Ehrlich Tumor (enzymology, metabolism)
  • DNA Polymerase I (antagonists & inhibitors, metabolism)
  • DNA Polymerase II (metabolism)
  • DNA Repair
  • DNA Replication
  • DNA-Binding Proteins (isolation & purification, physiology)
  • Enzyme Activation
  • Neoplasm Proteins (physiology)
  • T-Phages (enzymology)
  • Tumor Cells, Cultured (enzymology, metabolism)

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