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Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases.


ABSTRACT: Replicative DNA polymerases (DNAPs) move along template DNA in a processive manner. The structural basis of the mechanism of translocation has been better studied in the A-family of polymerases than in the B-family of replicative polymerases. To address this issue, we have determined the X-ray crystal structures of phi29 DNAP, a member of the protein-primed subgroup of the B-family of polymerases, complexed with primer-template DNA in the presence or absence of the incoming nucleoside triphosphate, the pre- and post-translocated states, respectively. Comparison of these structures reveals a mechanism of translocation that appears to be facilitated by the coordinated movement of two conserved tyrosine residues into the insertion site. This differs from the mechanism employed by the A-family polymerases, in which a conserved tyrosine moves into the templating and insertion sites during the translocation step. Polymerases from the two families also interact with downstream single-stranded template DNA in very different ways.

SUBMITTER: Berman AJ 

PROVIDER: S-EPMC1933411 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

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Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases.

Berman Andrea J AJ   Kamtekar Satwik S   Goodman Jessica L JL   Lázaro José M JM   de Vega Miguel M   Blanco Luis L   Salas Margarita M   Steitz Thomas A TA  

The EMBO journal 20070705 14


Replicative DNA polymerases (DNAPs) move along template DNA in a processive manner. The structural basis of the mechanism of translocation has been better studied in the A-family of polymerases than in the B-family of replicative polymerases. To address this issue, we have determined the X-ray crystal structures of phi29 DNAP, a member of the protein-primed subgroup of the B-family of polymerases, complexed with primer-template DNA in the presence or absence of the incoming nucleoside triphospha  ...[more]

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