Linked Life Data

11112487

Source:http://linkedlifedata.com/resource/pubmed/id/11112487

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-1-2
pubmed:abstractText
Our previous biochemical studies of HIV-1 and MuLV virions isolated and identified mature Gag products, HIV-1 p6(Gag) and MuLV p12(Gag), that were conjugated to a single ubiquitin. To study the importance of the monoubiquitination of Gag, a series of lysine to arginine mutants were constructed that eliminated ubiquitination at one or both of the lysines in HIV-1(NL4-3) p6(Gag) and both lysines in Moloney MuLV p12(Gag). HPLC and immunoblot analysis of the HIV-1 mutants demonstrated that either of the lysines in p6(Gag), K27 or K33, could be monoubiquitinated. However, infectivity assays showed that monoubiquitination of HIV-1 p6(Gag) or MuLV p12(Gag) is not required for viral replication in vitro. Pulse-chase radiolabeling of HIV-1-producing cells revealed that monoubiquitination of p6(Gag) does not affect the short-term release of virus from the cell, the maturation of Pr55(Gag), or the sensitivity of these processes to proteasome inhibitors. Experiments with protease-deficient HIV-1 showed that Pr55(Gag) can be monoubiquitinated, suggesting that p6(Gag) is first modified as a domain within Gag. Examination of the proteins inside an HIV-1 mutant found that free ubiquitin was incorporated into the virions in the absence of the lysines in p6(Gag), showing that the ubiquitin inside the virus is not initially brought in as a p6(Gag) conjugate. Although our results establish that monoubiquitination of p6(Gag) and p12(Gag) is not required for viral replication in vitro, this modification may be a by-product of interactions between Gag and cellular proteins during assembly and budding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0042-6822
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-21
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11112487-Amino Acid Sequence, pubmed-meshheading:11112487-Amino Acid Substitution, pubmed-meshheading:11112487-Animals, pubmed-meshheading:11112487-Arginine, pubmed-meshheading:11112487-Cell Line, pubmed-meshheading:11112487-Chromatography, High Pressure Liquid, pubmed-meshheading:11112487-Gene Products, gag, pubmed-meshheading:11112487-HIV Protease, pubmed-meshheading:11112487-HIV-1, pubmed-meshheading:11112487-Humans, pubmed-meshheading:11112487-Immunoblotting, pubmed-meshheading:11112487-Lysine, pubmed-meshheading:11112487-Mice, pubmed-meshheading:11112487-Molecular Sequence Data, pubmed-meshheading:11112487-Moloney murine leukemia virus, pubmed-meshheading:11112487-Mutagenesis, Site-Directed, pubmed-meshheading:11112487-Protein Precursors, pubmed-meshheading:11112487-Ubiquitins, pubmed-meshheading:11112487-Virus Replication, pubmed-meshheading:11112487-gag Gene Products, Human Immunodeficiency Virus
pubmed:year
2000
pubmed:articleTitle
Ubiquitination of HIV-1 and MuLV Gag.
pubmed:affiliation
AIDS Vaccine Program, SAIC Frederick, National Cancer Institute, Frederick, Maryland 21702-1201, USA. ott@avpvx1.ncifcrf.gov
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't