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Structural Basis of Polymerase Fidelity

Structural Basis of Polymerase Fidelity
聚合酶保真度的结构基础
批准号:
7734473
负责人:
JOHN W. DRAKE
金额:
$2.63万
依托单位国家:
美国
项目类别:
财政年份:
--
资助国家:
美国
项目状态:
未结题
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英文摘要
The RB69 DNA polymerase binding-pocket residue Tyr567 was shown previously to be a key determinant of fidelity: the replacement Y567A causes a powerful mutator activity. Ser565 is a nearby component of the binding pocket. Unlike Y567A, the replacement S565G has only a small impact on fidelity. However, combining Y567A and S565G reverses most of the mutator activity of Y567A. This is a unique and instructive observation in structural studies of polymerase fidelity, and we are working through a detailed examination of the mutational propensities of these constructs both in vivo and in vitro.
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