DNA polymerase δ and ζ switch by sharing accessory subunits of DNA polymerase δ

Andrey G. Baranovskiy, Artem G. Lada, Hollie M. Siebler, Yinbo Zhang, Youri I. Pavlov, Tahir H. Tahirov

Research output: Contribution to journalArticle

103 Scopus citations

Abstract

Translesion DNA synthesis is an important branch of the DNA damage tolerance pathway that assures genomic integrity of living organisms. The mechanisms of DNA polymerase (Pol) switches during lesion bypass are not known. Here, we show that the C-terminal domain of the Pol ζ catalytic subunit interacts with accessory subunits of replicative DNA Pol δ. We also show that, unlike other members of the human B-family ofDNApolymerases, the highly conserved and similar C-terminal domains of Pol δ and Pol ζ contain a [4Fe-4S] cluster coordinated by four cysteines. Amino acid changes in Polζ that prevent the assembly of the [4Fe-4S] cluster abrogate Pol ζ function in UV mutagenesis. On the basis of these data, we propose that Pol switches at replication-blocking lesions occur by the exchange of the Pol δand Pol ζ catalytic subunits on a preassembled complex of accessory proteins retained on DNA during translesion DNA synthesis.

Original languageEnglish (US)
Pages (from-to)17281-17287
Number of pages7
JournalJournal of Biological Chemistry
Volume287
Issue number21
DOIs
StatePublished - May 18 2012

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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