An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome

Arkadiusz W. Kulczyk, Barak Akabayov, Seung Joo Lee, Mihnea Bostina, Steven A. Berkowitz, Charles C. Richardson

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Synthesis of the leading DNA strand requires the coordinated activity of DNA polymerase and DNA helicase, whereas synthesis of the lagging strand involves interactions of these proteins with DNA primase. We present the first structural model of a bacteriophage T7 DNA helicase-DNA polymerase complex using a combination of small angle x-ray scattering, single-molecule, and biochemical methods. We propose that the proteinprotein interface stabilizing the leading strand synthesis involves two distinct interactions: a stable binding of the helicase to the palm domain of the polymerase and an electrostatic binding of the carboxyl-terminal tail of the helicase to a basic patch on the polymerase. DNA primase facilitates binding of DNA helicase to ssDNA and contributes to formation of the DNA helicase-DNA polymerase complex by stabilizing DNA helicase.

Original languageEnglish
Pages (from-to)39050-39060
Number of pages11
JournalJournal of Biological Chemistry
Volume287
Issue number46
DOIs
StatePublished - 9 Nov 2012
Externally publishedYes

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