Mutations in a CCHC zinc-binding motif of the reovirus sigma 3 protein decrease its intracellular stability.
It has been demonstrated that the sigma 3 protein of reovirus harbors a zinc-binding domain in its amino-terminal portion. A putative zinc finger in the CCHH form is located in this domain and was considered to be a good candidate for the zinc-binding motif. We performed site-directed mutagenesis to substitute amino acids in this region and demonstrated that many of these mutants, although expressed in COS cells, were unstable compared with the wild-type protein. Further analysis revealed that zinc-binding capability, as measured by retention on a zinc chelate affinity adsorbent, correlates with stability. These studies also allowed us to identify a CCHC box as the most probable zinc-binding motif.
Mabrouk
T
T
Département de Microbiologie et Immunologie, Université de Montréal, Québec, Canada.
Lemay
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G
D000595:Amino Acid Sequence; D000818:Animals; D036022:Capsid Proteins; D002460:Cell Line; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D016601:RNA-Binding Proteins; D012087:Reoviridae / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*
D036022:Capsid Proteins; D016601:RNA-Binding Proteins; D014764:Viral Proteins; C053179:sigma protein 3, Reovirus; D015032:Zinc