An Interaction between DNA Polymerase and Helicase is Essential for the High Processivity of the Bacteriophage T7 Replisome.

Abstract:

Synthesis of the leading DNA strand requires the coordinated activity of DNA polymerase and DNA helicase while 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 SAXS, single-molecule and biochemical methods. We propose that the protein-protein 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 C-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.

Polymerases:

T7

Topics:

Accessory Proteins/Complexes

Status:

new topics/pols set partial results complete validated

Results:

Polymerase Reference Property Result Context
T7 Kulczyk AW2012 Other accessory protein(s) helicase

Entry validated by:

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