Biomaterial Database

The RNA-binding site of bacteriophage Qbeta coat protein. 1996

F Lim, and M Spingola, and D S Peabody

Department of Cell Biology, University of New Mexico School of Medicine, and Cancer Research and Treatment Center, Albuquerque, New Mexico 87131, USA. dpeabody@cobra.unm.edu

The coat proteins of the RNA bacteriophages Qbeta and MS2 are specific RNA binding proteins. Although they possess common tertiary structures, they bind different RNA stem loops and thus provide useful models of specific protein-RNA recognition. Although the RNA-binding site of MS2 coat protein has been extensively characterized previously, little is known about Qbeta. Here we describe the isolation of mutants that define the RNA-binding site of Qbeta coat protein, showing that, as with MS2, it resides on the surface of a large beta-sheet. Mutations are also described that convert Qbeta coat protein to the RNA binding specificity of MS2. The results of these and other studies indicate that, although they bind different RNAs, the binding sites of the two coat proteins are sufficiently similar that each is easily converted by mutation to the RNA binding specificity of the other.

UI	MeSH Term	Description	Entries
D009690	Nucleic Acid Conformation	The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.	DNA Conformation,RNA Conformation,Conformation, DNA,Conformation, Nucleic Acid,Conformation, RNA,Conformations, DNA,Conformations, Nucleic Acid,Conformations, RNA,DNA Conformations,Nucleic Acid Conformations,RNA Conformations
D009875	Operator Regions, Genetic	The regulatory elements of an OPERON to which activators or repressors bind thereby effecting the transcription of GENES in the operon.	Operator Region,Operator Regions,Operator, Genetic,Genetic Operator,Genetic Operator Region,Genetic Operator Regions,Genetic Operators,Operator Region, Genetic,Operators, Genetic,Region, Genetic Operator,Region, Operator,Regions, Genetic Operator,Regions, Operator
D002213	Capsid	The outer protein protective shell of a virus, which protects the viral nucleic acid. Capsids are composed of repeating units (capsomers or capsomeres) of CAPSID PROTEINS which when assembled together form either an icosahedral or helical shape.	Procapsid,Prohead,Capsids,Procapsids,Proheads
D003090	Coliphages	Viruses whose host is Escherichia coli.	Escherichia coli Phages,Coliphage,Escherichia coli Phage,Phage, Escherichia coli,Phages, Escherichia coli
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012367	RNA, Viral	Ribonucleic acid that makes up the genetic material of viruses.	Viral RNA
D016296	Mutagenesis	Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.	Mutageneses
D017909	Levivirus	A bacteriophage genus of the family LEVIVIRIDAE, whose viruses contain the short version of the genome and have a separate gene for cell lysis.	Bacteriophage MS2,Coliphage MS2,Enterobacteria phage MS2,Enterobacteria phage R17,Enterobacteria phage f2,Enterobacteria phage fr,MS2 Phage,Phage MS2,Pseudomonas phage PP7,Leviviruses,MS2 Phages,MS2, Bacteriophage,MS2, Coliphage,MS2, Phage,Phage, MS2,Phages, MS2
D036022	Capsid Proteins	Proteins that form the CAPSID of VIRUSES.	Procapsid Protein,Procapsid Proteins,Viral Coat Protein,Viral Coat Proteins,Viral V Antigens,Viral V Proteins,Capsid Protein,Viral Outer Coat Protein,Antigens, Viral V,Coat Protein, Viral,V Antigens, Viral,V Proteins, Viral