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Differential proteolytic activities of precursor and mature forms of the 24K proteinase of grapevine fanleaf nepovirus.

Abstract：

:The presence of a genome-linked protein (VPg) at the RNA 5'-end of the genome is a characteristic of different groups of animal and plant positive-sense single-stranded RNA viruses. These viruses express their structural and functional proteins from polyproteins that are sequentially processed by at least one viral proteinase. The grapevine fanleaf nepovirus 24K chymotrypsin-like cysteine proteinase, located between the VPg and the RNA polymerase in the RNA-1 encoded polyprotein P1, is active in its free form and in various precursors forms. The VPg proteinase precursor (VPg-Pro) constitutes a stable protein and its maturation in the reticulocyte lysate system occurs at a very low rate. Differences on cleavage activity were observed between the proteinase and its VPg-Pro precursor forms, depending upon the cleavage site considered. The proteinase alone has a greater cleavage efficiency than VPg-Pro at the Arg605/Gly606 and Cys257/Ala258 sites of polyprotein P2. On the other hand, the presumed Cys415/Ala416 site, present at the amino terminus of polyprotein P1, was preferentially cleaved by the VPg-Pro precursor. During their in vitro maturation, proteins containing the VPg proteinase-polymerase coding region or the proteinase-polymerase region were similar in their ability to cleave in cis between the proteinase and the RNA polymerase.

journal_name

Virology

journal_title

Virology

authors

Margis R,Viry M,Pinck M,Bardonnet N,Pinck L

doi

10.1006/viro.1994.1165

subject

Has Abstract

pub_date

1994-04-01 00:00:00

pages

79-86

issue

1

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(84)71165-2

journal_volume

200

pub_type

杂志文章

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