Linked Life Data

10329567

Source:http://linkedlifedata.com/resource/pubmed/id/10329567

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-6-23
pubmed:databankReference
pubmed:abstractText
To complement evidence for nucleoside triphosphate phosphohydrolase (NTPase), RNA helicase, RNA 5' triphosphate phosphohydrolase, and nucleic acid-binding activities by the core shell protein lambda1 of mammalian orthoreoviruses (reoviruses), we determined nucleotide sequences of the lambda1-encoding L3 gene segments from three isolates: type 1 Lang (T1L), type 2 Jones (T2J), and type 3 Dearing (T3D). The T1L and T3D L3 gene sequences and deduced lambda1 protein sequences shared high levels of identity (97.7% and 99.3%, respectively). The lambda1 sequences differed at only 9 of 1275 amino acids. Two single-nucleotide insertions relative to a previously published sequence for T3D L3 extended the lambda1 open reading frame to within 60 nucleotides of the plus-strand 3' end for T3D and the other isolates sequenced, in keeping with the short 3' nontranslated regions of the other nine gene segments. Seven of the nine amino acid differences between T1L and T3D lambda1 were located within the amino-terminal 500 residues of lambda1, a region with putative sequence similarities to NTPases and RNA helicases. The T2J L3 and lambda1 sequences were found to be more divergent, especially within the amino-terminal 180 residues of lambda1, preceding the putative CCHH zinc finger motif. The T2J L3 sequence, along with partial sequences for L3 genes from three other reovirus isolates, suggested that one or more of the polymorphisms at amino acids 71, 215, 500, 1011, and/or 1100 in lambda1 contribute to the L3-determined differences in ATPase activities by T1L and T3D cores. The findings contribute to our ongoing efforts to elucidate sequence-structure-function relationships for the lambda1 core protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0042-6822
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
54-64
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10329567-Adenosine Triphosphatases, pubmed-meshheading:10329567-Amino Acid Sequence, pubmed-meshheading:10329567-Animals, pubmed-meshheading:10329567-Base Sequence, pubmed-meshheading:10329567-Capsid, pubmed-meshheading:10329567-Capsid Proteins, pubmed-meshheading:10329567-DNA, Viral, pubmed-meshheading:10329567-DNA-Binding Proteins, pubmed-meshheading:10329567-Gene Expression, pubmed-meshheading:10329567-Genes, Viral, pubmed-meshheading:10329567-Mammalian orthoreovirus 3, pubmed-meshheading:10329567-Mammals, pubmed-meshheading:10329567-Molecular Sequence Data, pubmed-meshheading:10329567-Mutagenesis, Insertional, pubmed-meshheading:10329567-Orthoreovirus, pubmed-meshheading:10329567-Peptide Chain Termination, Translational, pubmed-meshheading:10329567-Phenotype, pubmed-meshheading:10329567-RNA-Binding Proteins, pubmed-meshheading:10329567-Sequence Analysis, DNA
pubmed:year
1999
pubmed:articleTitle
Mammalian reovirus L3 gene sequences and evidence for a distinct amino-terminal region of the lambda1 protein.
pubmed:affiliation
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't