DNA POLYMERASE STRUCTURES

DNA聚合酶结构

• 批准号: 7955201
• 负责人: Tahir H Tahirov
• 金额: $ 0.22万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-04-01 至 2010-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955201
• 关键词: Active Sites; Amino Acids; Binding; C-terminal; Catalytic Domain; Complex; Computer Retrieval of Information on Scientific Projects Database; DBL Oncoprotein; DNA; DNA Repair; DNA-Directed DNA Polymerase; Funding; Genome; Goals; Grant; Human; Institution; Mediating; Metabolism; N-terminal; Phosphodiesterase I; Play; Polymerase; Proteins; Regulation; Research; Research Personnel; Resources; Role; Screening procedure; Source; TNFRSF5 gene; United States National Institutes of Health; homologous recombination; scaffold; structural biology; yeast two hybrid system

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The eukaryotic DNA polymerase ¿ (Pol ¿) participates in genome replication, homologous recombination, DNA repair and damage tolerance. Human Pol ¿ consists of four subunits: p125, p50, p66, and p12. The largest catalytic subunit contains the polymerase and 3'¿5' exonuclease active sites domains. No catalytic activity is associated with the auxiliary p50, p66, and p12 subunits, and they are thought to play a regulatory role, stimulate the polymerase activity of p125 by mediating additional interactions with PCNA, and stabilize the entire Pol ¿ complex. p50 serves as a scaffold for the assembly of Pol ¿ by interacting simultaneously with all of the other three subunits. In addition, p50 is also involved in the recruitment of several proteins regulating DNA metabolism, including p21, PDIP1, PDIP38, PDIP46 and WRN. The parts of p50 responsible for interactions with p66, p125 and p12 have not been defined. Using two-hybrid screening, the human p66 has been shown to contain p50- and PCNA-binding domains within the 144 N- and 20 C-terminal amino acids, respectively. Interestingly, many essential functions of Pol ¿, including the regulation of replication, TLS and BIR, are mediated by the p66 subunit and thus apparently depend on the interaction between its p50 and p66 subunits. The goal of this subproject is to study the complex between the p50 subunit and the 144 amino acids N-terminal domain of the third p66 subunit (p66N) of human Pol ¿.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中央赠款提供的资源 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此，在列出的机构中可能会被压制 对于中心，这不一定是调查员的工厂。 真核DNA聚合酶» （pol�）参与基因组复制，同源重组，DNA修复和损伤耐受性。由四个亚基组成：p125，p50，p66和p12。 5'EXONUCELE活性位点结构域。复合物。通过与所有其他亚基同时相互作用，p50也是p21，pdip1，pdip38，pdip46和p5的部分人p66分别包含P50和PCNA结合域，分别具有氨基酸。 ，包括复制，TLS和BIR的调节，由p66亚基介导，显然取决于其P50和66个亚基之间的相互作用。人类pol的第三个p66亚基（p66n）的N末端结构域。