home
***
CD-ROM
|
disk
|
FTP
|
other
***
search
/
The Arsenal Files 6
/
The Arsenal Files 6 (Arsenal Computer).ISO
/
health
/
med9604b.zip
/
M9640609.TXT
< prev
next >
Wrap
Text File
|
1996-03-04
|
3KB
|
40 lines
Document 0609
DOCN M9640609
TI Phosphorylation-dependent human immunodeficiency virus type 1 infection
and nuclear targeting of viral DNA.
DT 9604
AU Bukrinskaya AG; Ghorpade A; Heinzinger NK; Smithgall TE; Lewis RE;
Stevenson M; Department of Pathology and Microbiology, University of
Nebraska; Medical Center, Omaha 68198-5120, USA.
SO Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):367-71. Unique Identifier :
AIDSLINE MED/96133938
AB In the replication of human immunodeficiency virus type 1 (HIV-1), gag
MA (matrix), a major structural protein of the virus, carries out
opposing targeting functions. During virus assembly, gag MA is
cotranslationally myristoylated, a modification required for membrane
targeting of gag polyproteins. During virus infection, however, gag MA,
by virtue of a nuclear targeting signal at its N terminus, facilitates
the nuclear localization of viral DNA and establishment of the provirus.
We now show that phosphorylation of gag MA on tyrosine and serine prior
to and during virus infection facilitates its dissociation from the
membrane, thus allowing it to translocate to the nucleus. Inhibition of
gag MA phosphorylation either on tyrosine or on serine prevents gag
MA-mediated nuclear targeting of viral nucleic acids and impairs virus
infectivity. The requirement for gag MA phosphorylation in virus
infection is underscored by our finding that a serine/threonine kinase
is associated with virions of HIV-1. These results reveal a novel level
of regulation of primate lentivirus infectivity.
DE Base Sequence Cell Compartmentation Cell Membrane/METABOLISM Cell
Nucleus/METABOLISM DNA Primers/CHEMISTRY DNA, Viral/*METABOLISM Gene
Products, gag/*METABOLISM Hela Cells Human HIV-1/ENZYMOLOGY/*GROWTH &
DEVELOPMENT/GENETICS Molecular Sequence Data Myristates/METABOLISM
Phosphoproteins/METABOLISM Phosphorylation Phosphoserine/METABOLISM
Phosphotyrosine/METABOLISM Protein-Serine-Threonine Kinases/ANTAGONISTS
& INHIB Protein-Tyrosine Kinase/ANTAGONISTS & INHIB Support, Non-U.S.
Gov't Support, U.S. Gov't, P.H.S. Viral Matrix Proteins/*METABOLISM
Virion/ENZYMOLOGY *Virus Replication JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).