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Title

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

AuthorsBerman, Andrea J.; Kamtekar, S.; Goodman, J. L.; Lázaro, José M. ; Vega, Miguel de ; Blanco, Luis ; Salas, Margarita ; Steitz, T. A.
KeywordsDNA polymerase
Phi29
Issue Date2007
PublisherNature Publishing Group
CitationEmbo Journal 26:3494 - 3505 (2007)
AbstractReplicative 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.
Publisher version (URL)http://dx.doi.org/10.1038/sj.emboj.7601780
URIhttp://hdl.handle.net/10261/37767
DOI10.1038/sj.emboj.7601780
ISSN0261-4189
Appears in Collections:(CBM) Artículos
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