A crystallographic study of the role of sequence context in thymine glycol bypass by a replicative DNA polymerase serendipitously sheds light on the exonuclease complex.
A crystallographic study of the role of sequence context in thymine glycol bypass by a replicative DNA polymerase serendipitously sheds light on the exonuclease complex.
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DOI:
10.1016/j.jmb.2011.07.007
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发表时间:
2011-09-09
影响因子:
5.6
通讯作者:
Doublié S
中科院分区:
文献类型:
--
作者:
Aller P;Duclos S;Wallace SS;Doublié S
Thymine glycol (Tg) is the most common oxidation product of thymine and is known to be a strong block for replicative DNA polymerases. A previously solved structure of the bacteriophage RB69 DNA polymerase (RB69 gp43) in complex with Tg in the sequence context 5’-G-Tg-G shed light on how Tg blocks primer elongation: The protruding methyl group of the oxidized thymine displaces the adjacent 5’-G which can no longer serve as a template for primer elongation. [Aller, P., Rould, M.A., Hogg, M, Wallace, S.S., & Doublié S. (2007) PNAS 104, 814–818] Several studies showed that in the 5’-C-Tg-Purine sequence context Tg is more likely to be bypassed by Klenow fragment, a family A DNA polymerase. We set out to investigate the role of sequence context on Tg bypass in a B family polymerase and solved the crystal structures of the bacteriophage RB69 DNA polymerase in complex with Tg containing DNA in the three remaining sequence contexts: 5’-N-Tg-G with N=A, T, or C. A combination of several factors influence Tg bypass, including the associated exonuclease activity, the nature of the 3’and 5’ bases surrounding Tg and the cis/trans interconversion of Tg. We also visualized for the first time the structure of a well-ordered exonuclease complex, allowing us to identify and confirm the role of key residues (Phe123, Met256, and Tyr257) in strand separation and the stabilization of the primer strand in the exonuclease site.
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影响因子:
4.8
作者:
Elisseeva, E;Mandal, SS;Reha-Krantz, LJ
通讯作者:
Reha-Krantz, LJ
影响因子:
14.9
作者:
CLARK, JM;BEARDSLEY, GP
通讯作者:
BEARDSLEY, GP
DOI:
10.1107/s0907444998003254
发表时间:
1998-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Brunger, AT;Adams, PD;Warren, GL
通讯作者:
Warren, GL
影响因子:
11.4
作者:
BEESE, LS;STEITZ, TA
通讯作者:
STEITZ, TA
影响因子:
2.9
作者:
Aller, Pierre;Ye, Yu;Wallace, Susan S.;Burrows, Cynthia J.;Doublie, Sylvie
通讯作者:
Doublie, Sylvie