Source:http://linkedlifedata.com/resource/pubmed/id/11336555
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2001-5-4
|
pubmed:abstractText |
The paramyxovirus P protein is an essential component of the viral RNA polymerase composed of P and L proteins. In this study, we characterized the physical and functional interactions between P and L proteins using human parainfluenza virus type 1 (hPIV1) and its counterpart Sendai virus (SV). The hPIV1 P and SV L proteins or the SV P and hPIV1 L proteins formed complexes detected by anti-P antibodies. Functional analysis using the minigenome SV RNA containing CAT gene indicated that the hPIV1 P--SV L complex, but not the SV P--hPIV1 L complex, was biologically active. Mutant SV P or hPIV1 P cDNAs, which do not express C proteins, showed the same phenotype with wild-type P cDNAs, indicating that C proteins are not responsible for the dysfunction of SV P--hPIV1 L polymerase complex. Using the chimeric hPIV1/SV P cDNAs, we identified two regions (residues 387--423 and 511--568) on P protein, which are required for the functional interaction with hPIV1 L. These regions overlap with a previously identified domain for oligomer formation and binding to nucleocapsids. Our results indicate that in addition to a P--L binding domain, hPIV1 L requires a specific region on P protein to be biologically functional as a polymerase.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/L protein, Sendai virus,
http://linkedlifedata.com/resource/pubmed/chemical/P protein, parainfluenza virus 1,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nonstructural C protein, Sendai...
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0042-6822
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
283
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
306-14
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11336555-Amino Acid Sequence,
pubmed-meshheading:11336555-DNA-Directed RNA Polymerases,
pubmed-meshheading:11336555-HeLa Cells,
pubmed-meshheading:11336555-Humans,
pubmed-meshheading:11336555-Molecular Sequence Data,
pubmed-meshheading:11336555-Nucleocapsid,
pubmed-meshheading:11336555-Parainfluenza Virus 1, Human,
pubmed-meshheading:11336555-Phosphoproteins,
pubmed-meshheading:11336555-Respirovirus,
pubmed-meshheading:11336555-Transfection,
pubmed-meshheading:11336555-Viral Proteins
|
pubmed:year |
2001
|
pubmed:articleTitle |
Two regions of the P protein are required to be active with the L protein for human parainfluenza virus type 1 RNA polymerase activity.
|
pubmed:affiliation |
Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale St., Memphis, Tennessee 38105-2794, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|