Cofactors for human immunodeficiency virus type 1 cDNA integration in vitro.

Szczegóły
Abstrakt

Tytuł:: Cofactors for human immunodeficiency virus type 1 cDNA integration in vitro.
Autorzy:: Gao K; Infectious Disease Laboratory, The Salk Institute, La Jolla, California 92037, USA.
Gorelick RJ
Johnson DG
Bushman F
Źródło:: Journal of virology [J Virol] 2003 Jan; Vol. 77 (2), pp. 1598-603.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
Język:: English
Imprint Name(s):: Publication: Washington Dc : American Society For Microbiology
Original Publication: Baltimore, American Society for Microbiology.
MeSH Terms:: HIV-1/*genetics
Virus Integration/*genetics
Base Sequence ; DNA, Complementary ; DNA-Binding Proteins/physiology ; HIV Long Terminal Repeat
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Grant Information:: N01CO12400 United States CA NCI NIH HHS; R01 AI034786 United States AI NIAID NIH HHS; AI34786 United States AI NIAID NIH HHS; GM56553 United States GM NIGMS NIH HHS
Substance Nomenclature:: 0 (DNA, Complementary)
0 (DNA-Binding Proteins)
Entry Date(s):: Date Created: 20021228 Date Completed: 20030122 Latest Revision: 20190508
Update Code:: 20240104
PubMed Central ID:: PMC140775
DOI:: 10.1128/jvi.77.2.1598-1603.2003
PMID:: 12502875
: Czasopismo naukowe

We have investigated the function of two DNA binding proteins that stimulate human immunodeficiency virus type 1 cDNA integration in vitro, the cellular HMGa1 protein and the viral nucleocapsid (NC) protein. Of the three forms of NC (NCp7, NCp9, and NCp15), we find that NCp9 is the most effective at increasing integration in vitro; thus, processing of NC may potentially modulate its activities during infection. We also found that maximal stimulation by NCp9 required roughly enough NC to coat the reactant DNAs whereas less HMGa1 was required, and the reactions displayed different optima for divalent metal cofactors and order of addition. These findings reveal probable distinct mechanisms of action in vitro.

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