课题基金 / 基金详情

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

项目摘要

项目成果

JOHN W. DRAKE的其他基金

相似基金

相关文献

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导致强大的突变活性。Ser565是结合口袋的邻近组分。与Y567A不同，替代品S565G对保真度的影响很小。然而，组合Y567A和S565G逆转了Y567A的大部分增变子活性。这是一个独特的和有益的观察聚合酶保真度的结构研究，我们正在通过详细检查这些结构在体内和体外的突变倾向。
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.
期刊论文(0)
专著(0)
科研奖励(0)
会议论文
Direct Isolation of Chromosomal Regions for the Study of Human Genes
Structural Basis of Polymerase Fidelity
Replication Repair
Structural Basis Of Polymerase Fidelity
海外基金