Linked Life Data

9391060

Source:http://linkedlifedata.com/resource/pubmed/id/9391060

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1998-1-15
pubmed:abstractText
HIV type 1 (HIV-1) specifically uses host cell tRNALys-3 as a primer for reverse transcription. The 3' 18 nucleotides of this tRNA are complementary to a region on the HIV RNA genome known as the primer binding site (PBS). HIV-1 has a strong preference for maintaining a lysine-specific PBS in vivo, and viral genomes with mutated PBS sequences quickly revert to be complementary to tRNALys-3. To investigate the mechanism for the observed PBS reversion events in vitro, we examined the capability of the nucleocapsid protein (NC) to anneal various tRNA primer sequences onto either complementary or noncomplementary PBSs. We show that NC can anneal different full-length tRNAs onto viral RNA transcripts derived from the HIV-1 MAL or HXB2 isolates, provided that the PBS is complementary to the tRNA used. In contrast, NC promotes specific annealing of only tRNALys-3 onto an RNA template (HXB2) whose PBS sequence has been mutated to be complementary to the 3' 18 nt of human tRNAPro. Moreover, HIV-1 reverse transcriptase extends this binary complex from the proline-specific PBS. The formation of the noncomplementary binary complex does not occur when a chimeric tRNALys/Pro containing proline-specific D and anticodon domains is used as the primer. Thus, elements outside the acceptor-TPsiC domains of tRNALys-3 play an important role in preferential primer use in vitro. Our results support the hypothesis that mutant PBS reversion is a result of tRNALys-3 annealing onto and extension from a PBS that specifies an alternate host cell tRNA.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-1280240, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-1324434, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-1551877, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-1627125, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-1631144, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-1705120, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-1714513, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-2430190, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-2476069, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-2479543, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-3277187, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-3277950, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-3684574, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-509527, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7503978, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7508999, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7511112, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7521916, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7522561, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7538660, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7543198, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7545240, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7687348, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7707372, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7707537, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7829498, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-7966556, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8057466, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8373592, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8429553, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8497049, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8551637, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8602365, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8621554, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8631312, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8764006, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8806524, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-8985340, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-9159468, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-9169409, http://linkedlifedata.com/resource/pubmed/commentcorrection/9391060-9223461
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13530-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The nucleocapsid protein specifically anneals tRNALys-3 onto a noncomplementary primer binding site within the HIV-1 RNA genome in vitro.
pubmed:affiliation
University of Minnesota, Department of Chemistry, 207 Pleasant Street SE, Minneapolis, MN 55455, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't