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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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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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