Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma3
By atomic absorption analysis, the authors determined that the reovirus outer capsid protein sigma3, which binds double-stranded RNA (dsRNA), is a zinc metalloprotein. Using Northwestern blots and a novel zinc blotting technique, the authors localized the zinc- and dsRNA-binding activities of sigma3 to distinct V8 protease-generated fragments. Zinc-binding activity was contained within an amino-terminal fragment that contained a transcription factor IIIA-like zinc-binding sequence, and dsRNA-binding activity was associated with a carboxy-terminal fragment. By these techniques, new zinc- and dsRNA-binding activities were also detected in reovirus core proteins. A sequence similarity was observed between the catalytic site of the picornavirus proteases and the transcription factor IIIA-like zinc-binding site within sigma3. The authors suggest that the zinc- and dsRNA-binding activities of sigma3 may be important for its proposed regulatory effects on viral and host cell transcription and translation.
- Research Organization:
- Dept. of Microbiology and Molecular Genetics, Harvard Medical School (US)
- OSTI ID:
- 6925572
- Journal Information:
- Mol. Cell. Biol.; (United States), Vol. 8:1
- Country of Publication:
- United States
- Language:
- English
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37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
METALLOPROTEINS
AMINO ACID SEQUENCE
MOLECULAR STRUCTURE
NUCLEOPROTEINS
TRANSCRIPTION FACTORS
VIRUSES
MOLECULAR BIOLOGY
ANIMAL CELLS
CHEMICAL ANALYSIS
CHEMICAL REACTION KINETICS
ELECTROPHORESIS
RNA
ZINC
ELEMENTS
KINETICS
METALS
MICROORGANISMS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PROTEINS
REACTION KINETICS
550200* - Biochemistry
400201 - Chemical & Physicochemical Properties