RNA PROTEIN INTERACTIONS IN E COLI RHO

本文主要研究大肠杆菌rna结合结构域的结构和特异性蛋白-核苷酸相互作用。ρ蛋白质。该蛋白在原核生物的转录终止中起重要作用。Rho特别有趣，因为它能很好地结合单链DNA和单链DNA，然而，它只有在与RNA结合时才被激活。核磁共振波谱方法将用于确定rho RNA结合域与单链RNA和单链DNA结合时的结构。将利用各种寡核苷酸配体和蛋白质突变来探索蛋白质与核酸之间的具体相互作用，进一步了解rho依赖性转录终止的分子机制。近年来，人们对DNA结合蛋白有了很多了解，但对RNA结合蛋白的了解相对较少。表征rho与核酸的结合相互作用将有助于理解RNA在其他蛋白质中的结合，因为RNA结合域与许多原核和真核RNA结合蛋白具有结构同源性。

This proposal focuses on the investigation of structure, and specific protein-nucleotide interactions of the RNA-binding domain of E. coli. rho protein. This protein plays an important role in the termination of transcription in prokaryotic organisms. Rho is particularly intriguing in that it binds equally well single- stranded DNA and single-stranded DNA however, it is only activated when bound to RNA. NMR spectroscopy methods will be used to determine the structures of-the rho RNA binding domain when bound to single stranded RNA and single stranded DNA. Various oligonucleotide ligands and protein mutations will be used to probe the specific interactions between the protein and nucleic acids to further the understand molecular mechanism of rho-dependent transcription termination. While much has been learned about DNA binding protein in recent years, relatively little is known about RNA binding proteins. Characterization of the binding interactions of rho with nucleic acids will be helpful in understanding RNA binding in other proteins since the RNA binding domain has structural homology with many prokaryotic and eukaryotic RNA-binding proteins.