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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1996-11-5
pubmed:abstractText
Influenza virus RNA polymerase with the subunit structure PB1-PB2-PA is involved in both transcription and replication of the RNA genome. By transfection of various combinations of cDNA encoding wild-type and serial deletion mutants of each P protein subunit and co-immunoprecipitation with subunit-specific antibodies, the subunit-subunit contact sites on all three of the P proteins were determined. Results indicate that binary complexes are formed between PB1-PB2 and PB1-PA but not between PB2-PA. Therefore, we concluded that PB1 is the core subunit for assembly of the virus RNA polymerase. The C-terminal 158 amino acids of PB1 bound to the N-terminal 249 amino acids of PB2, while the N-terminal 140 amino acids of PB1 bound to the C-terminal two-thirds of PA. PB2-PA binding was not detected when they were expressed in the absence of the PB1 subunit.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
77 ( Pt 9)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2149-57
pubmed:dateRevised
2007-10-11
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Molecular assembly of the influenza virus RNA polymerase: determination of the subunit-subunit contact sites.
pubmed:affiliation
Department of Molecular Genetics, National Institute of Genetics, Shizuoka, Japan. ttoyoda@ddbj.nig.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't