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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：
7968077
负责人：
JOHN W. DRAKE
金额：
$1.42万
依托单位：
NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES
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
起止时间：
至
来源：
https://reporter.nih.gov/project-details/7968077
关键词：
Active SitesAmino AcidsAutomobile DrivingBacteriophage T4BacteriophagesBindingCongenital AbnormalityDNA biosynthesisDNA-Directed DNA PolymeraseDiseaseEnzymesExonucleaseFamilyGeneticGerm LinesHealthIn VitroInduced MutationMaintenanceMalignant NeoplasmsMutationPlasmidsPolymeraseSomatic CellStructureSystemTestingWorkbacteriophage RB69 DNA polymerasebasehuman DNAin vitro testingin vivomitochondrial dysfunctionmutantreplicasespleen exonuclease

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中文摘要
翻译
RB69 DNA聚合酶结合口袋残基Tyr567先前被证明是保真度的关键决定因素，因为替换Y567A导致了强大的突变子活性。Ser565是捆绑袋的附近组件。与Y567A不同的是，更换后的S565G对保真度的影响很小。然而，结合Y567A和S565G可以逆转Y567A的大部分突变子活性。这在聚合酶保真度的结构研究中是一个独特和有指导意义的观察结果，我们正在对这些结构在体内和体外的突变倾向进行详细的检查。
英文摘要
The RB69 DNA polymerase binding-pocket residue Tyr567 was shown previously to be a key determinant of fidelity because 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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