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呼肠孤病毒σ3蛋白的CCHC锌结合基序中的突变会降低其细胞内稳定性。

Mutations in a CCHC zinc-binding motif of the reovirus sigma 3 protein decrease its intracellular stability.

作者信息

Mabrouk T, Lemay G

机构信息

Département de Microbiologie et Immunologie, Université de Montréal, Québec, Canada.

出版信息

J Virol. 1994 Aug;68(8):5287-90. doi: 10.1128/JVI.68.8.5287-5290.1994.

DOI:10.1128/JVI.68.8.5287-5290.1994
PMID:8035527
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC236476/
Abstract

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.

摘要

已经证明呼肠孤病毒的σ3蛋白在其氨基末端部分含有一个锌结合结构域。该结构域中存在一个假定的CCHH形式的锌指，被认为是锌结合基序的良好候选者。我们进行了定点诱变以替换该区域中的氨基酸，并证明许多这些突变体尽管在COS细胞中表达，但与野生型蛋白相比不稳定。进一步分析表明，通过在锌螯合亲和吸附剂上的保留来衡量的锌结合能力与稳定性相关。这些研究还使我们能够确定一个CCHC框是最可能的锌结合基序。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6046/236476/ccc72807f090/jvirol00017-0595-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6046/236476/266fcd9574a1/jvirol00017-0594-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6046/236476/fa1df3fc8d4e/jvirol00017-0594-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6046/236476/ccc72807f090/jvirol00017-0595-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6046/236476/266fcd9574a1/jvirol00017-0594-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6046/236476/fa1df3fc8d4e/jvirol00017-0594-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6046/236476/ccc72807f090/jvirol00017-0595-a.jpg

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