The synthesis and processing of the nepovirus grapevine fanleaf virus proteins in rabbit reticulocyte lysate

Morris-Krsinich, Bret A.M.; Forster, R. L. S.; Mossop, D.W.

doi:10.1016/0042-6822(83)90105-8

Cited by 21 publications

(20 citation statements)

References 13 publications

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“…(ii) The sequence flanking the second AUG codon is in better agreement with the consensus sequence determined by Kozak (1981) for translation initiation codons than is that flanking the first AUG. (iii) After subtraction of 56K corresponding to the coat protein from the 122K or the 131K polyprotein either 66K or 75K remain for the Nterminal part of this protein. The value of 66K is in good agreement with the 68K protein found in the translation products of GFLV RNA2 in reticulocyte lysates by Morris-Krsinich et al (1983).…”

Section: Determination Of the Sequence Of Rna2supporting

confidence: 74%

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RNA2 of grapevine fanleaf virus: sequence analysis and coat protein cistron location

Serghini

Fuchs

Pinck

et al. 1990

Journal of General Virology

129

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The nucleotide sequence of the genomic RNA2 (3774 nucleotides) of grapevine fanleaf virus strain F13 was determined from overlapping cDNA clones and its genetic organization was deduced. Two rapid and efficient methods were used for cDNA cloning of the 5' region of RNA2. The complete sequence contained only one long open reading frame of 3555 nucleotides (1184 codons, 131K product). The analysis of the Nterminal sequence of purified coat protein (CP) and identification of its C-terminal residue have allowed the CP cistron to be precisely positioned within the polyprotein. The CP produced by proteolytic cleavage at the Arg/Gly site between residues 680 and 681 contains 504 amino acids (Mr 56019) and has hydrophobic properties. The Arg/Gly cleavage site deduced by N-terminal amino acid sequence analysis is the first for a nepovirus coat protein and for plant viruses expressing their genomic RNAs by polyprotein synthesis. Comparison of GFLV RNA2 with M RNA of cowpea mosaic comovirus and with RNA2 of two closely related nepoviruses, tomato black ring virus and Hungarian grapevine chrome mosaic virus, showed strong similarities among the 3' non-coding regions but less similarity among the 5' end non-coding sequences than reported among other nepovirus RNAs.

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Section: Determination Of the Sequence Of Rna2supporting

confidence: 74%

“…In the absence of these analogues, a specific protease induced by RNA1 catalysed the cleavage of the 125K protein into two proteins of 68K and 58K. Peptide mapping after partial proteolysis of the 58K protein strongly suggested that it was the viral coat protein (Morris-Krsinich et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

RNA2 of grapevine fanleaf virus: sequence analysis and coat protein cistron location

Serghini

Fuchs

Pinck

et al. 1990

Journal of General Virology

129

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“…Thus the 250 kDa protein potentially encoded by GCMV RNA1 is a polyprotein. This is confirmed by in vitro translation results showing that the primary translation product of GCMV RNA I is processed (G. Demangeat, personal communication), as also described for other nepoviruses (4,14).…”

Section: Nucleic Acids Researchsupporting

confidence: 62%

Nucleotide sequence of Hungarian grapevine chrome mosaic nepovirus RNA1

Gall¹,

Candresse²,

Brault³

et al. 1989

Nucl Acids Res

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The nucleotide sequence of the RNAl of hungarian grapevine chrome mosaic virus, a nepovirus very closely related to tomato black ring virus, has been determined from cDNA clones. It is 7212 nucleotides in length excluding the 3' terminal poly(A) tail and contains a large open reading frame extending from nucleotides 216 to 6971. The presumably encoded polyprotein is 2252 amino acids in length with a molecular weight of 250 kDa. The primary structure of the polyprotein was compared with that of other viral polyproteins, revealing the same general genetic organization as that of other picorna-like viruses (comoviruses, potyviruses and picornaviruses), except that an additional protein is suspected to occupy the N-terminus of the polyprotein.

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“…Thus the 253K protein potentially encoded by GFLV RNA1 is a polyprotein. This is confirmed by an in vitro translation experiment showing that the primary translation product of GFLV RNA1 is processed (Morris-Krsinich et al, 1983) as has also been shown for other nepoviruses (Fritsch et al, 1980;Forster & Morris-Krsinich, 1985;Demangeat et al, 1990). To map the mature viral proteins on the precursor, we aligned the RNAl-encoded polyprotein (253K) with that encoded by other nepoviruses TBRV (254K) and GCMV (250K), comoviruses (CPMV, 200K) and a picornavirus (HPV, 247K) using computer-assisted sequence comparison with the software of Devereux et al (1984).…”

Section: Sequence Homologies Between Rna1 and Rna2 Of Gfl V And Othermentioning

confidence: 48%

“…Studies on the distribution of genetic functions between genome segments of nepoviruses have shown that RNAI is able to replicate independently in protoplasts (Robinson et al, 1980) and thus encodes the information necessary for viral replication. Moreover, in vitro processing studies have shown that the RNA 1-encoded polyprotein is able to catalyse the cleavage of the 122K protein into two proteins of 68K and 58K and thus contains a protease activity (Morris-Krsinich et at., 1983). The coat protein (CP) cistron has been precisely positioned within the polyprotein encoded by RNA2 and it has been shown that the CP (Mr 56K) is produced by proteolytic cleavage of the 122K polyprotein at an Arg/Gly site (Serghini et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Complete nucleotide sequence and genetic organization of grapevine fanleaf nepovirus RNA1

Ritzenthaler

Viry

Pinck

et al. 1991

Journal of General Virology

109

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The nucleotide sequence of the genomic RNA 1, 7342 nucleotides (nt) of grapevine fanleaf virus strain F13 (GFLV-FI 3) has been determined from cDNA clones. The complete sequence contained only one long open reading frame (ORF) of 6852 nucleotides extending from nucleotide 243 to 7101. The putative polyprotein encoded by this ORF is 2284 amino acids in length with an Mr of 253K. The location of genome-linked protein and comparison of the primary structure of the 253K polyprotein to that of other closely related viral proteins of the picornavirus-like family allows the proposal of a scheme for the genetic organization of GFLV-FI3 RNAI. The primary structure of the polyprotein includes a putative RNA-dependent RNA polymerase of 92K and a cysteine protease of 25K. This protease shares not only major structural homologies, particularly in the snbstrate-binding pocket, with the trypsin-like serine proteases of other picorna-like viruses, but also their specificity in terms of cleavage. The large region of Mr 133K upstream of the VPg was found to contain at least two domains, one of which could be easily aligned with the NTP-binding sequence pattern and another which may have the characteristics of a protease eofactor. Thus, the 253K protein possesses the same general genetic organization as the corresponding protein of other picorna-like viruses.

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The synthesis and processing of the nepovirus grapevine fanleaf virus proteins in rabbit reticulocyte lysate

Cited by 21 publications

References 13 publications

RNA2 of grapevine fanleaf virus: sequence analysis and coat protein cistron location

RNA2 of grapevine fanleaf virus: sequence analysis and coat protein cistron location

Nucleotide sequence of Hungarian grapevine chrome mosaic nepovirus RNA1

Complete nucleotide sequence and genetic organization of grapevine fanleaf nepovirus RNA1

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