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Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus.

Abstract：

:The interaction between the nucleocapsid (N) protein of mouse hepatitis virus (MHV) and RNA was studied in an effort to define portions of the N molecule that participate in binding to RNA. N mRNAs transcribed from SP6 and T7 vectors were translated in a rabbit reticulocyte lysate. Analysis of synthesized N protein in a nondenaturing gel system showed that it bound in vitro to an endogenous RNA in the reticulocyte lysate but not to its own mRNA. A set of deletion mutants was constructed in order to localize the RNA-binding activity of the N protein. It was found that removal of as much as 135 amino-terminal or 57 carboxy-terminal amino acids from the molecule had little or no effect on RNA binding. Moreover, deletion mutants lacking both termini still retained RNA-binding ability. By contrast, internal deletions or truncations extending beyond these two limits effectively abolished RNA binding by N protein. Thus, the RNA-binding region of N has been mapped to the second (central) of the three structural domains of the molecule.

journal_name

Arch Virol

journal_title

Archives of virology

authors

Masters PS

doi

10.1007/BF01309634

keywords:

subject

Has Abstract

pub_date

1992-01-01 00:00:00

pages

141-60

issue

1-4

eissn

0304-8608

issn

1432-8798

journal_volume

125

pub_type

杂志文章

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