منابع مشابه
Purification of RNA and RNA-protein complexes by an R17 coat protein affinity method.
We describe an affinity chromatography method to isolate specific RNAs and RNA-protein complexes formed in vivo or in vitro. It exploits the highly selective binding of the coat protein of bacteriophage R17 to a short hairpin in its genomic RNA. RNA containing that hairpin binds to coat protein that has been covalently bound to a solid support. Bound RNA-protein complexes can be eluted with exc...
متن کاملRNA binding properties of the coat protein from bacteriophage GA.
The coat protein of bacteriophage GA, a group II RNA phage, binds to a small RNA hairpin corresponding to its replicase operator. Binding is specific, with a Ka of 71 microM -1. This interaction differs kinetically from the analogous coat protein-RNA hairpin interactions of other RNA phage and also deviates somewhat in its pH and salt dependence. Despite 46 of 129 amino acid differences between...
متن کاملMS 2 coat protein mutants which bind Q β RNA
The coat proteins of the RNA phages MS2 and Qβ are structurally homologous, yet they specifically bind different RNA structures. In an effort to identify the basis of RNA binding specificity we sought to isolate mutants that convert MS2 coat protein to the RNA binding specificity of Qβ. A library of mutations was created which selectively substitutes amino acids within the RNA binding site. Gen...
متن کاملDissecting protein–RNA recognition sites
We analyze the protein-RNA interfaces in 81 transient binary complexes taken from the Protein Data Bank. Those with tRNA or duplex RNA are larger than with single-stranded RNA, and comparable in size to protein-DNA interfaces. The protein side bears a strong positive electrostatic potential and resembles protein-DNA interfaces in its amino acid composition. On the RNA side, the phosphate contri...
متن کاملMapping of the RNA recognition site of Escherichia coli ribosomal protein S7.
Bacterial ribosomal protein S7 initiates the folding of the 3' major domain of 16S ribosomal RNA by binding to its lower half. The X-ray structure of protein S7 from thermophilic bacteria was recently solved and found to be a modular structure, consisting of an alpha-helical domain with a beta-ribbon extension. To gain further insights into its interaction with rRNA, we cloned the S7 gene from ...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2002
ISSN: 1362-4962
DOI: 10.1093/nar/gkf552