Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1992-1-7
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M65138,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M65139,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S64909,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S64910,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S64911,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S64912,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S64914,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S64915,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S67553,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S67557
|
pubmed:abstractText |
The complete nucleotide sequences of the RNA-1 segments in broad bean mottle virus (BBMV) and cowpea chlorotic mottle virus (CCMV) were determined. BBMV RNA-1 consists of 3158 nucleotides and CCMV RNA-1 has 3171 nucleotides. Both BBMV and CCMV RNA-1 are capped at the 5' end but, unlike in other tricornaviruses, BBMV RNA-1 initiates with an A residue. Both BBMV and CCMV RNA-1 are monocistronic encoding for highly homologous 1a proteins of 966 and 958 amino acids, respectively. The highest homologies are clustered within two domains: the N-domain that aligns with the nsP1 Sindbis virus protein, a putative methyl transferase, and the C-domain which has a conserved nucleotide binding motif. Previous sequence comparisons suggest that the C-terminal domain may function as an NTP-dependent RNA helicase. In addition, we find that the C-domain has patterns similar to those of the reovirus and vaccinia virus guanylyl transferases. All this implies that 1a protein is a multifunctional polypeptide involved in both RNA capping and RNA polymerization processes.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0042-6822
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
185
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
553-62
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1962437-Amino Acid Sequence,
pubmed-meshheading:1962437-Base Sequence,
pubmed-meshheading:1962437-Cloning, Molecular,
pubmed-meshheading:1962437-Consensus Sequence,
pubmed-meshheading:1962437-Genome, Viral,
pubmed-meshheading:1962437-Molecular Sequence Data,
pubmed-meshheading:1962437-Open Reading Frames,
pubmed-meshheading:1962437-Plant Viruses,
pubmed-meshheading:1962437-RNA Viruses,
pubmed-meshheading:1962437-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1962437-Viral Proteins
|
pubmed:year |
1991
|
pubmed:articleTitle |
The nucleotide sequence and genome organization of the RNA-1 segment in two bromoviruses: broad bean mottle virus and cowpea chlorotic mottle virus.
|
pubmed:affiliation |
Northern Illinois University, Department of Biological Sciences, DeKalb 60115.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|