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Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage phi29.

Abstract：

:The DNA polymerase from phage phi29 is a B family polymerase that initiates replication using a protein as a primer, attaching the first nucleotide of the phage genome to the hydroxyl of a specific serine of the priming protein. The crystal structure of phi29 DNA polymerase determined at 2.2 A resolution provides explanations for its extraordinary processivity and strand displacement activities. Homology modeling suggests that downstream template DNA passes through a tunnel prior to entering the polymerase active site. This tunnel is too small to accommodate double-stranded DNA and requires the separation of template and nontemplate strands. Members of the B family of DNA polymerases that use protein primers contain two sequence insertions: one forms a domain not previously observed in polymerases, while the second resembles the specificity loop of T7 RNA polymerase. The high processivity of phi29 DNA polymerase may be explained by its topological encirclement of both the downstream template and the upstream duplex DNA.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Kamtekar S,Berman AJ,Wang J,Lázaro JM,de Vega M,Blanco L,Salas M,Steitz TA

doi

10.1016/j.molcel.2004.10.019

subject

Has Abstract

pub_date

2004-11-19 00:00:00

pages

609-18

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(04)00645-8

journal_volume

16

pub_type

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