Nucleotide sequence of the open reading frames adjacent to the coat protein cistron in potato virus X genome

Abstract

The cloned cDNA copies corresponding to 1300 nucleotides adjacent to the 3'-terminal poly(A) tract of the potato virus X (PVX) genome have been sequenced. The amino acid sequences of three open reading frames were deduced from the nucleotide sequence. Two putative small nonstructura1 polypeptides corresponding to the open reading frames adjacent to the coat protein cistron possess some properties of membrane-associated proteins. Direct sequence homology and common structural peculiarities exist between the PVX small proteins and the putative small nonstructural proteins encoded by RNA 2 of hordeiviruses and furoviruses cDNA; Cloning; Amino acid sequence; Sequence homology; Membrane-bound protein; (Plant virus)

Nicotiana Velutina Mosaic Virus: Evidence for a Bipartite Genome Comprising 3 kb and 8 kb RNAs

“…5). This highly conserved sequence is flanked by blocks of hydrophobic residues which suggest an association with membranes in infected cells as noted before for the corresponding proteins of BNYVV, BSMV and PVX (Morozov et al, 1987(Morozov et al, , 1989. Similarities are also observed between NVMV ORF 4 and the BNYVV 15K, BSMV 17K and PVX 8K proteins, respectively (data not shown).…”

“…6) indicate that there is marked conservation of genes between viruses of this type. Thus, by analogy, the presence of hydrophobic segments on the putative 13K polypeptide indicate a possible association with membranes (Morozov et al, 1987). The NTPbinding motif in the NVMV 39K polypeptide may have a role in unwinding double-stranded replicative forms during genomic RNA replication (Morozov et at., 1989).…”

Highlights and prospects of potyvirus molecular biology

“…The primary function of CP is, obviously, to encapsidate viral RNA, a process in which the highly conserved central and C-terminal regions characteristic of potyviral CPs are likely to be involved (Shukla & Ward, 1989b). In fact, the C-terminal part of potyvirus CPs shares sequence similarity with the CPs of the otherwise unrelated (in terms of genomic structure and strategy of expression) filamentous plant viruses potex-, carla-, clostero-and tobamoviruses (Morozov et al, 1987;Lain et al, 1988;Dinant et al, 1991). The molecular characterization of particle assembly and genome encapsidation processes would be facilitated by the recent development of microbial (E. coli and yeast) assembly systems (Jagadish et al, 1991).…”

Partial Nucleotide Sequence of Potato Virus M RNA Shows Similarities to Potexviruses in Gene Arrangement and the Encoded Amino Acid Sequences

“…Morozov et al (1987) noted that several non-virion proteins of positive-sense RNA-containing plant viruses (potyviruses and carmoviruses) contain highly hydrophobic segments and might be membrane-bound. Small non-virion proteins of potexviruses, hordeiviruses and furoviruses are also hydrophobic and could interact directly with membranes (Morozov et al, , 1989Forster et al, 1988).…”