共 45 条
Structure of Saccharomyces cerevisiae DNA polymerase epsilon by cryo-electron microscopy
被引:83
作者:

Asturias, FJ
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机构: Scripps Res Inst, Dept Biol Struct, La Jolla, CA 92037 USA

Cheung, IK
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机构: Scripps Res Inst, Dept Biol Struct, La Jolla, CA 92037 USA

Sabouri, N
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机构: Scripps Res Inst, Dept Biol Struct, La Jolla, CA 92037 USA

Chilkova, O
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机构: Scripps Res Inst, Dept Biol Struct, La Jolla, CA 92037 USA

Wepplo, D
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机构: Scripps Res Inst, Dept Biol Struct, La Jolla, CA 92037 USA

Johansson, E
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机构: Scripps Res Inst, Dept Biol Struct, La Jolla, CA 92037 USA
机构:
[1] Scripps Res Inst, Dept Biol Struct, La Jolla, CA 92037 USA
[2] Umea Univ, Dept Med Biochem & Biophys, SE-90187 Umea, Sweden
关键词:
D O I:
10.1038/nsmb1040
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The structure of the multisubunit yeast DNA polymerase epsilon (Pol epsilon) was determined to 20-angstrom resolution using cryo- EM and single-particle image analysis. A globular domain comprising the catalytic Pol2 subunit is flexibly connected to an extended structure formed by subunits Dpb2, Dpb3 and Dpb4. Consistent with the reported involvement of the latter in interaction with nucleic acids, the Dpb portion of the structure directly faces a single cleft in the Pol2 subunit that seems wide enough to accommodate double-stranded DNA. Primer-extension experiments reveal that Pol e processivity requires a minimum length of primer-template duplex that corresponds to the dimensions of the extended Dpb structure. Together, these observations suggest a mechanism for interaction of Pol e with DNA that might explain how the structure of the enzyme contributes to its intrinsic processivity.
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页码:35 / 43
页数:9
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