STRUCTURE AND FUNCTION OF A PEPTIDE OF BROME MOSAIC VIRUS IN MEMBRANE BINDING

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 雀麦花叶病毒（BMV）蛋白1a是一种多功能RNA复制因子，在病毒RNA复制复合物的组装和功能中起关键作用。1a作为外周膜蛋白定位于核周内质网（ER）膜，诱导ER膜内陷，其中RNA复制发生，并募集BMV 2a聚合酶和RNA复制模板以形成RNA复制复合物。我们在1a中鉴定了一种肽，该肽与1a与ER膜的功能相关。突变研究表明，特定的残基的肽是重要的1A协会与膜。因此，在上述结果的基础上，我们将使用NMR来确定该肽的三维结构及其与膜结合的机制。

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. Brome Mosaic Virus (BMV) protein 1a is a multifunctional RNA replication factor with key roles in assembly and function of viral RNA replication complexes. 1a localizes to perinuclear endoplasmic reticulum (ER) membranes as a peripheral membrane protein, induces ER membrane invaginations in which RNA replication occurs, and recruits BMV 2a polymerase and RNA replication templates to form RNA replication complexes. We identified a peptide in 1a that is critically involved in 1a's functional association with ER membranes. Mutational studies showed that specific residues of the peptide were important for 1a association with membranes. Accordingly, to build on the above results, we will use NMR to determine the three dimensional structure of this peptide and the mechanism of its binding to membranes.