1999
DOI: 10.1099/0022-1317-80-3-799
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Proteolytic processing of tomato ringspot nepovirus 3C-like protease precursors: definition of the domains for the VPg, protease and putative RNA-dependent RNA polymerase.

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Cited by 30 publications
(49 citation statements)
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“…In vitro, the ToRSV NTB-VPg cleavage site is a predominant cis-cleavage site, and accumulation of NTB-VPg is not detected. Rather, the mature NTB and the VPg-Pro intermediate were shown to accumulate (54,55). The accumulation of NTB-VPg in infected plants suggests that cellular factors (such as the membrane environment) modulate the recognition of the NTB-VPg cleavage site by the ToRSV proteinase.…”
Section: Discussionmentioning
confidence: 99%
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“…In vitro, the ToRSV NTB-VPg cleavage site is a predominant cis-cleavage site, and accumulation of NTB-VPg is not detected. Rather, the mature NTB and the VPg-Pro intermediate were shown to accumulate (54,55). The accumulation of NTB-VPg in infected plants suggests that cellular factors (such as the membrane environment) modulate the recognition of the NTB-VPg cleavage site by the ToRSV proteinase.…”
Section: Discussionmentioning
confidence: 99%
“…1A) (43). The proteinase processes P1 at five cleavage sites in vitro, and the precise locations of the NTB-VPg, VPg-Pro, and Pro-Pol cleavage sites have been determined experimentally (54,55). The NTB protein has sequence elements similar to those found in known RNA helicases (24) and has homology with the picornavirus 2C and 3A proteins.…”
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confidence: 98%
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“…It has been observed earlier that in some viruses, VPg influences the activity of the protease. For instance, in Tomato ringspot nepovirus (TomRSV), VPg-Pro precursor was shown to be more active in cleavage at one of the sites (4). In cowpea mosaic virus, expression of the protease along with the N-terminal extension corresponding to the VPg sequence enhanced its proteolytic activity (5).…”
mentioning
confidence: 99%
“…The genome of Tomato ringspot nepovirus (ToRSV) consists of two molecules of RNA (45). RNA1 encodes a polyprotein (P1) containing the domains for the replication proteins, including the RNA-dependent RNA polymerase, a 3C-like proteinase, the genome-linked protein (VPg), a putative nucleoside triphosphate-binding protein (NTB), and two additional proteins (X1 and X2) of unknown function (42,59,61). The 3C-like proteinase is responsible for cleavage of P1 and of the RNA2-encoded polyprotein (13).…”
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confidence: 99%