IDENTIFYING THE PATH OF THE RNA PRIMER AROUND A SIMPLE RNA POLYMERASE

识别简单 RNA 聚合酶周围 RNA 引物的路径

基本信息

批准号：
7954492
负责人：
CHANGGONG LI
金额：
$ 0.33万
依托单位：
STANFORD UNIVERSITY
依托单位国家：
美国
项目类别：
财政年份：
2009
资助国家：
美国
起止时间：
2009-03-01 至 2010-02-28
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/7954492
关键词：
Binding Sites Complex Computer Retrieval of Information on Scientific Projects Database DNA-Directed RNA Polymerase Ensure Funding Grant Hour Individual Institution Polymerase Polynucleotide Adenylyltransferase Proteins RNA RNA Polymerase I RNA primers Research Research Personnel Resources Source Structure Surface Tail Time United States National Institutes of Health Vaccinia virus Work flexibility structural biology synchrotron radiation

Binding Sites Complex Computer Retrieval of Information on Scientific Projects Database DNA-Directed RNA Polymerase Ensure Funding Grant Hour Individual Institution Polymerase Polynucleotide Adenylyltransferase Proteins RNA RNA Polymerase I RNA primers Research Research Personnel Resources Source Structure Surface Tail Time United States National Institutes of Health Vaccinia virus Work flexibility structural biology synchrotron radiation

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项目摘要

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. Vaccinia virus poly(A) polymerase (VP55) is the only RNA polymerase known to translocate with respect to its RNA primer, raising a paradox: Which is more flexible: The polymerase or the primer? The protein has two known modes of action, namely the processive synthesis of 30 nt tails and, as a heterodimer with its processivity factor (VP39), the semi-processive synthesis of 200 ? 300 nt tails. Past, collaborative studies, have yielded crystal structures for VP39, and for the VP55-VP39 heterodimer. The most important, yet absent information is a structural understanding of the heterodimer-primer complex. By using the beam time of a colleague, a full-time crystallographer in the Gershon lab has progressed markedly in finding binding sites for short RNA segments on the polymerase surface. Although this is ground-breaking, original work for a poly(A) polymerase, 3 hours of beam time every 2 months provides inadequate progress in this NIH-funded work to ensure grant renewal. Beam time is the major bottleneck, hence the current request for individual, regular beam time for this crystallographic work.

该副本是利用众多研究子项目之一由NIH/NCRR资助的中心赠款提供的资源。子弹和调查员（PI）可能已经从其他NIH来源获得了主要资金，因此可以在其他清晰的条目中代表。列出的机构是对于中心，这不一定是调查员的机构。 Vacinia病毒聚（A）聚合酶（VP55）是唯一已知相对于其RNA底漆的RNA聚合酶，提高了悖论：哪个更灵活：聚合酶或底漆？该蛋白质具有两种已知的作用模式，即30 nt尾巴的过程合成，并且作为具有其加工性因子的异二聚体（VP39），是200的半配学合成？ 300 nt尾巴。过去的协作研究已经为VP39和VP55-VP39异二聚体产生了晶体结构。最重要但缺乏信息是对异二聚体络合物复合物的结构理解。通过使用同事的光束时间，Gershon Lab中的一名全职晶体学家在发现聚合酶表面上短RNA片段的结合位点方面取得了显着发展。尽管这是开创性的，是聚（A）聚合酶的原始作品，但每2个月的3个小时的光束时间在这项NIH资助的工作中提供了不足的进度，以确保授予续签。光束时间是主要的瓶颈，因此当前对此晶体学工作的单个常规光束时间请求。