RNASE P

核糖核酸酶P

• 批准号: 8171431
• 负责人: DAVID R ENGELKE
• 金额: $ 0.24万
• 依托单位: UNIVERSITY OF WASHINGTON
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-09-01 至 2011-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8171431
• 关键词: Affinity; Computer Retrieval of Information on Scientific Projects Database; Funding; Grant; Holoenzymes; Institution; Lead; Nuclear; Process; Proteins; RNase P; Research; Research Personnel; Resources; Ribonucleases; Role; Source; United States National Institutes of Health; Work; Yeasts; novel

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 yeast nuclear RNase P is responsible for the maturation of the 5' end of precursor tRNAs. There are several lines of evidence that lead us to believe that RNase P has additional substrates and we have recently identified several candidiates. Work to attempt the identification of interacting partners outside the known core of RNase P is being carried out. Using novel affinity tags, we are able to rapidly isolate the holoenzyme and expect to find interacting proteins that were lost during the initial arduous purification that led to the identification of the RNase P core. These interacting partners will be investigated for their roles in the processing of novel substrate candidates recently identified in our lab.

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。 酵母核RNase P负责前体TRNA的5'末端的成熟。有几条证据使我们相信RNase P还有其他底物，我们最近确定了几个候选人。 正在尝试识别在RNase P的已知核心之外的互动伙伴的工作。使用新颖的亲和力标签，我们能够快速分离全酶，并期望在初始艰苦的纯化过程中找到丢失的相互作用蛋白，从而导致RNase P核心鉴定。这些相互作用的伙伴将在我们实验室最近确定的新型底物候选者处理中的作用。