FACTORS INFLUENCING GENETIC TRANSCRIPTION-INITIATION AND TERMINATION

影响基因转录起始和终止的因素

• 批准号: 3878032
• 负责人: R CROUCH
• 金额: --
• 依托单位: EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3878032
• 关键词: DNA directed RNA polymerase; Escherichia coli; RNA directed DNA polymerase; Retroviridae; bacterial genetics; enzyme mechanism; enzyme structure; gene expression; genetic manipulation; genetic transcription; hybrid enzyme; messenger RNA; molecular genetics; nucleic acid sequence; protein engineering; protein sequence; protein structure function; ribonuclease III; ribosomal RNA; transcription factor; transcription termination

Analysis of the crystal structure of E. coli RNase H indicates a protein of a five-stranded beta-sheet surrounded by five alpha-helices. Conserved, essential carboxylic acid amino acids probably bind Mg++ and thereby initiate an interaction between the enzyme and the substrate. These negatively charged, conserved amino acids converge with other conserved residues on one face of the molecule. Retroviral and yeast RNase HI have additional domains which may affect the location and/or function of their RNases H. The RNase H domain of yeast functions without the remainder of the protein whereas the retroviral RNase H exhibits a requirement for most of the polymerase domain for maximal activity.

对E.大肠杆菌RNase H表明， 一个五股β折叠被五个α螺旋包围保存， 必需的羧酸氨基酸可能与Mg++结合， 引发酶和底物之间的相互作用。这些 带负电荷的保守氨基酸与其他保守氨基酸会聚， 在分子的一面上的残基。逆转录病毒和酵母RNase HI具有 可能影响其位置和/或功能的其他域 核糖核酸酶H.酵母的RNase H结构域的功能没有其余的 而逆转录病毒RNA酶H表现出对大多数蛋白质的需求， 以获得最大活性。