The nuclear matrix protein, MATR3, is a newly-described Rev cofactor whose mechanism of action is only starting to be revealed

A Kula

Andrew I Dayton

AS Cockrell

AS Zolotukhin

AW Cochrane

CA Rosen

FD Bushman

H Nakayasu

HC Groom

JM Cronshaw

M Buxade

M Suhasini

MJ Zeitz

P Belgrader

S Hisada-Ishii

S Kameoka

VSRK Yedavalli

Y Shav-Tal

Z Zhang

Retrovirology

English

PubMed

Springer - Publisher Connector

COMMENTARY Open Access
Matrin 3 and HIV Rev Regulation of mRNA
Andrew I Dayton
Abstract
The nuclear matrix protein, MATR3, is a newly-described Rev cofactor whose mechanism of action is only starting
to be revealed.
Introduction
Retroviruses by necessity have evolved mechanisms to
export unspliced viral genomic and mRNA out of the
nucleus and into the cytoplasm, where they can be trans-
lated or assembled into virions. The first such system dis-
covered was the Rev/Rev Response Element (RRE) system
in HIV-1. The paradigm proposed for Rev/RRE function
[1], whereby interaction of Rev with the RRE (originally
known as CAR, for Cis Anti-Repressor) overcomes cis
repressor sequences (CRS, or INS - inhibitory sequences)
that otherwise retain unspliced/partially spliced mRNA
within the nucleus, has proven remarkably durable. The
early debates over whether Rev acts by splicing inhibition
(allowing export) or by rapid export (kinetically outracing
splicing and/or degradation), have devolved to a more
complex picture, in which Rev interacts with the RRE and
with CRM-1/exportin 1, which in turn interacts with the
phenylalanine-glycine (FG) repeats of nucleoporins, med-
iating export. Once in the cytoplasm, Rev-dependent
mRNAs, in some systems, may also require Rev for effi-
cient translation (reviewed in [2]). Multiple factors have
been reported to interact directly or indirectly with Rev-
mediated mRNA transport/expression (reviewed in [3]).
Furthermore, proposals for how CRS sequences block
incompletely spliced viral RNA from productive export
have invoked message instability, or message retention -
the latter from suboptimal splicing or binding to nuclear
factors (reviewed in [4]). Whatever the mechanisms
involved, the effects of the Rev/RRE interaction are only
apparent when the mRNA contains CRS/INS sequences.
Discussion
Two papers recently co-published in this journal [5,6]
implicate the nuclear matrix protein, MATR3, as a
co-factor used by the HIV-1 Rev protein to facilitate the
nuclear export and translation of unspliced and partially
spliced viral mRNA. The Marcello group came to this dis-
covery using MS2 coat protein recognition sequence tags
and MS2 pull down to survey host proteins specifically
bound to HIV mRNA. The Jeang lab came to it through a
yeast 2 hybrid survey of proteins that bound to PTB-1
("polypyrimidine tract binding protein-1”), reasoning that,
since PSF (a “PTB-1 associated splicing factor”) inhibits
the expression of CRS/INS-containing HIV-1 transcripts
[7], other PTB-1 binding proteins, such as MATR3, might
do so as well. Remarkably, these two divergent histories
led to agreement on the facts at hand:
• MATR3 binds intracellularly to HIV mRNA.
• MATR3 has no direct effect on transcription from
the HIV LTR despite its previous (though admittedly
weak) implication in a role in transcription [8-11].
• For maximal function, Rev needs MATR3 to pro-
mote the cytoplasmic accumulation and (presumably
consequent) translation of unspliced (or partially
spliced) RRE-containing mRNA.
• Rev, MATR3 and RRE-containing mRNA form a
detectable intracellular complex.
The addition of MATR3 to the pantheon of Rev
cofactors is tantalizing: MATR3 exists in cells, com-
plexed with PSF and nrbp54 [12-15]; PSF binds to CRS/
INS sequences in HIV mRNA and suppresses the
expression of these RNAs ([7]); MATR3 has been identi-
fied as a constituent of the nuclear pore proteome [16].
Consequently, it is tempting to view Rev as working
with MATR3 to free mRNA from CRS retention (by, for
example, PSF), allowing export; or as working with
MATR3 to ferry mRNA to/through the nucleopore. The
two mechanisms need not be mutually exclusive.Correspondence: andrew.dayton@fda.hhs.gov
FDA/CBER/OBRR/DETTD/LMV, HFM 315 1401 Rockville Pike Rockville MD
20852-1448, USA
Dayton Retrovirology 2011, 8:62
http://www.retrovirology.com/content/8/1/62
© 2011 Dayton; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons
Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in
any medium, provided the original work is properly cited.
Figure 1 Parsimonious kinetic models of Rev export and different mechanisms of CRS/INS function. A) A typical cellular pre-mRNA, with
typical splicing sites, even with a heterologous RRE, is not exported by Rev. B) Introduction of a “retention” or “aberrant splicing” CRS/INS into a
mRNA retards splicing, allowing Rev/RRE export to effectively compete. C) Instability factors inducing degradation might be proposed to interact
directly with CRS/INS, but stability alone without retardation of splicing would still not allow Rev/RRE export the opportunity to compete. D)
Similarly, were Rev/RRE merely to release such an instability factor, rapid splicing would still outcompete Rev/RRE export, as in A. SD, splice
donor; SA, splice acceptor; E#, exon#.
Dayton Retrovirology 2011, 8:62
http://www.retrovirology.com/content/8/1/62
Page 2 of 3
Theoretically, the pre-translational effects of Rev can
be explained entirely by a simple transport mechanism
based on competitive kinetics. The involvement of Rev/
RRE in transport is well documented. What is important
to understand is that, as mentioned above, the effects of
Rev/RRE transport are only seen in the presence of
CRS/INS sequences. The logical consequence of this is
that any Rev mechanism must at least do more than
merely abolish CRS/INS interaction with the binding
partners responsible for repression. Otherwise, Rev
would merely render a target mRNA equivalent to a
typical mRNA which would be rapidly spliced and then
exported. As depicted in Figure 1, splicing of a typical
mRNA, even with an RRE, is too rapid for Rev to inter-
dict (Figure 1A). Any CRS/INS mechanism which makes
export of mRNA Rev-dependent must necessarily retard
splicing (Figure 1B) to allow Rev-export. Though degra-
dation may very well result from delayed splicing, any
CRS mechanism based totally on mRNA instability can
not work, because elimination of the instability would
still allow rapid splicing to outrace Rev-export (Figure 1,
C and 1D). Nevertheless, though parsimony does not
require more than export to be involved in Rev over-
coming CRS/INS inhibition and promoting cytoplasmic
expression of unspliced mRNA, there is nothing to say
that a multifunctional protein such as Rev does not also
get directly involved in prying mRNA from various
interacting partners which would otherwise contribute
to its retention, such as components of aberrant splicing
complexes. How MATR3 fits into any of these scenarios
remains to be determined.
Finally, MATR3 has also been identified as interacting
with the molecular chaperone cluster implicated by
siRNA screening to be involved in viral assembly [17].
This could underlie observations that Rev is involved in
encapsidation (see [18] and [2]).
Conclusions
As is generally the case, the answers to all of these ques-
tions will emerge as more information is obtained con-
cerning Rev/RRE and CRS/INS associated factors and
their normal cellular roles. At the age of 24, the field of
Rev remains rich and productive.
Competing interests
The author declares that they have no competing interests.
Received: 10 July 2011 Accepted: 20 July 2011 Published: 20 July 2011
References
1. Rosen CA, Terwilliger E, Dayton A, Sodroski JG, Haseltine WA: Intragenic
cis-acting art gene-responsive sequences of the human
immunodeficiency virus. Proc Natl Acad Sci USA 1988, 85:2071-2075.
2. Groom HC, Anderson EC, Lever AM: Rev: beyond nuclear export. J Gen
Virol 2009, 90:1303-1318.
3. Suhasini M, Reddy TR: Cellular proteins and HIV-1 Rev function. Curr HIV
Res 2009, 7:91-100.
4. Cochrane AW, McNally MT, Mouland AJ: The retrovirus RNA trafficking
granule: from birth to maturity. Retrovirology 2006, 3:18.
5. Yedavalli VSRK, Jang K-T: Matrin 3 is a co-factor for HIV-1 Rev in
regulating post-transcriptional viral gene expression. Retrovirology 2011,
8:61.
6. Kula A, Guerra J, Knezevich A, Kleva D, Michael D, Myers P, Marcello A:
Characterization of the HIV-1 RNA associated proteome identifies Matrin
3 as a nuclear cofactor of Rev function. Retrovirology 2011, 8:60.
7. Zolotukhin AS, Michalowski D, Bear J, Smulevitch SV, Traish AM, Peng R,
Patton J, Shatsky IN, Felber BK: PSF acts through the human
immunodeficiency virus type 1 mRNA instability elements to regulate
virus expression. Mol Cell Biol 2003, 23:6618-6630.
8. Belgrader P, Dey R, Berezney R: Molecular cloning of matrin 3. A 125-
kilodalton protein of the nuclear matrix contains an extensive acidic
domain. J Biol Chem 1991, 266:9893-9899.
9. Nakayasu H, Berezney R: Nuclear matrins: identification of the major
nuclear matrix proteins. Proc Natl Acad Sci USA 1991, 88:10312-10316.
10. Hisada-Ishii S, Ebihara M, Kobayashi N, Kitagawa Y: Bipartite nuclear
localization signal of matrin 3 is essential for vertebrate cells. Biochem
Biophys Res Commun 2007, 354:72-76.
11. Zeitz MJ, Malyavantham KS, Seifert B, Berezney R: Matrin 3: chromosomal
distribution and protein interactions. J Cell Biochem 2009, 108:125-133.
12. Zhang Z, Carmichael GG: The fate of dsRNA in the nucleus: a p54(nrb)-
containing complex mediates the nuclear retention of promiscuously A-
to-I edited RNAs. Cell 2001, 106:465-475.
13. Shav-Tal Y, Zipori D: PSF and p54(nrb)/NonO–multi-functional nuclear
proteins. FEBS Lett 2002, 531:109-114.
14. Kameoka S, Duque P, Konarska MM: p54(nrb) associates with the 5’ splice
site within large transcription/splicing complexes. Embo J 2004,
23:1782-1791.
15. Buxade M, Morrice N, Krebs DL, Proud CG: The PSF.p54nrb complex is a
novel Mnk substrate that binds the mRNA for tumor necrosis factor
alpha. J Biol Chem 2008, 283:57-65.
16. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ: Proteomic
analysis of the mammalian nuclear pore complex. J Cell Biol 2002,
158:915-927.
17. Bushman FD, Malani N, Fernandes J, D’Orso I, Cagney G, Diamond TL,
Zhou H, Hazuda DJ, Espeseth AS, Konig R, et al: Host cell factors in HIV
replication: meta-analysis of genome-wide studies. PLoS Pathog 2009, 5:
e1000437.
18. Cockrell AS, van Praag H, Santistevan N, Ma H, Kafri T: The HIV-1 Rev/RRE
system is required for HIV-1 5’ UTR cis elements to augment
encapsidation of heterologous RNA into HIV-1 viral particles.
Retrovirology 2011, 8:51.
doi:10.1186/1742-4690-8-62
Cite this article as: Dayton: Matrin 3 and HIV Rev Regulation of mRNA.
Retrovirology 2011 8:62.
Submit your next manuscript to BioMed Central
and take full advantage of: 
• Convenient online submission
• Thorough peer review
• No space constraints or color figure charges
• Immediate publication on acceptance
• Inclusion in PubMed, CAS, Scopus and Google Scholar
• Research which is freely available for redistribution
Submit your manuscript at 
www.biomedcentral.com/submit
Dayton Retrovirology 2011, 8:62
http://www.retrovirology.com/content/8/1/62
Page 3 of 3


Matrin 3 and HIV Rev Regulation of mRNA

Abstract The nuclear matrix protein, MATR3, is a newly-described Rev cofactor whose mechanism of action is only starting to be revealed.</p

Dayton Andrew I

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COMMENTARY Open AccessMatrin 3 and HIV Rev Regulation of mRNAAndrew I DaytonAbstractThe nuclear matrix protein, MATR3, is a newly-described Rev cofactor whose mechanism of action is only startingto be revealed.IntroductionRetroviruses by necessity have evolved mechanisms toexport unspliced viral genomic and mRNA out of thenucleus and into the cytoplasm, where they can be trans-lated or assembled into virions. The first such system dis-covered was the Rev/Rev Response Element (RRE) systemin HIV-1. The paradigm proposed for Rev/RRE function[1], whereby interaction of Rev with the RRE (originallyknown as CAR, for Cis Anti-Repressor) overcomes cisrepressor sequences (CRS, or INS - inhibitory sequences)that otherwise retain unspliced/partially spliced mRNAwithin the nucleus, has proven remarkably durable. Theearly debates over whether Rev acts by splicing inhibition(allowing export) or by rapid export (kinetically outracingsplicing and/or degradation), have devolved to a morecomplex picture, in which Rev interacts with the RRE andwith CRM-1/exportin 1, which in turn interacts with thephenylalanine-glycine (FG) repeats of nucleoporins, med-iating export. Once in the cytoplasm, Rev-dependentmRNAs, in some systems, may also require Rev for effi-cient translation (reviewed in [2]). Multiple factors havebeen reported to interact directly or indirectly with Rev-mediated mRNA transport/expression (reviewed in [3]).Furthermore, proposals for how CRS sequences blockincompletely spliced viral RNA from productive exporthave invoked message instability, or message retention -the latter from suboptimal splicing or binding to nuclearfactors (reviewed in [4]). Whatever the mechanismsinvolved, the effects of the Rev/RRE interaction are onlyapparent when the mRNA contains CRS/INS sequences.DiscussionTwo papers recently co-published in this journal [5,6]implicate the nuclear matrix protein, MATR3, as aco-factor used by the HIV-1 Rev protein to facilitate thenuclear export and translation of unspliced and partiallyspliced viral mRNA. The Marcello group came to this dis-covery using MS2 coat protein recognition sequence tagsand MS2 pull down to survey host proteins specificallybound to HIV mRNA. The Jeang lab came to it through ayeast 2 hybrid survey of proteins that bound to PTB-1("polypyrimidine tract binding protein-1”), reasoning that,since PSF (a “PTB-1 associated splicing factor”) inhibitsthe expression of CRS/INS-containing HIV-1 transcripts[7], other PTB-1 binding proteins, such as MATR3, mightdo so as well. Remarkably, these two divergent historiesled to agreement on the facts at hand:• MATR3 binds intracellularly to HIV mRNA.• MATR3 has no direct effect on transcription fromthe HIV LTR despite its previous (though admittedlyweak) implication in a role in transcription [8-11].• For maximal function, Rev needs MATR3 to pro-mote the cytoplasmic accumulation and (presumablyconsequent) translation of unspliced (or partiallyspliced) RRE-containing mRNA.• Rev, MATR3 and RRE-containing mRNA form adetectable intracellular complex.The addition of MATR3 to the pantheon of Revcofactors is tantalizing: MATR3 exists in cells, com-plexed with PSF and nrbp54 [12-15]; PSF binds to CRS/INS sequences in HIV mRNA and suppresses theexpression of these RNAs ([7]); MATR3 has been identi-fied as a constituent of the nuclear pore proteome [16].Consequently, it is tempting to view Rev as workingwith MATR3 to free mRNA from CRS retention (by, forexample, PSF), allowing export; or as working withMATR3 to ferry mRNA to/through the nucleopore. Thetwo mechanisms need not be mutually exclusive.Correspondence: andrew.dayton@fda.hhs.govFDA/CBER/OBRR/DETTD/LMV, HFM 315 1401 Rockville Pike Rockville MD20852-1448, USADayton Retrovirology 2011, 8:62http://www.retrovirology.com/content/8/1/62© 2011 Dayton; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative CommonsAttribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction inany medium, provided the original work is properly cited.Figure 1 Parsimonious kinetic models of Rev export and different mechanisms of CRS/INS function. A) A typical cellular pre-mRNA, withtypical splicing sites, even with a heterologous RRE, is not exported by Rev. B) Introduction of a “retention” or “aberrant splicing” CRS/INS into amRNA retards splicing, allowing Rev/RRE export to effectively compete. C) Instability factors inducing degradation might be proposed to interactdirectly with CRS/INS, but stability alone without retardation of splicing would still not allow Rev/RRE export the opportunity to compete. D)Similarly, were Rev/RRE merely to release such an instability factor, rapid splicing would still outcompete Rev/RRE export, as in A. SD, splicedonor; SA, splice acceptor; E#, exon#.Dayton Retrovirology 2011, 8:62http://www.retrovirology.com/content/8/1/62Page 2 of 3Theoretically, the pre-translational effects of Rev canbe explained entirely by a simple transport mechanismbased on competitive kinetics. The involvement of Rev/RRE in transport is well documented. What is importantto understand is that, as mentioned above, the effects ofRev/RRE transport are only seen in the presence ofCRS/INS sequences. The logical consequence of this isthat any Rev mechanism must at least do more thanmerely abolish CRS/INS interaction with the bindingpartners responsible for repression. Otherwise, Revwould merely render a target mRNA equivalent to atypical mRNA which would be rapidly spliced and thenexported. As depicted in Figure 1, splicing of a typicalmRNA, even with an RRE, is too rapid for Rev to inter-dict (Figure 1A). Any CRS/INS mechanism which makesexport of mRNA Rev-dependent must necessarily retardsplicing (Figure 1B) to allow Rev-export. Though degra-dation may very well result from delayed splicing, anyCRS mechanism based totally on mRNA instability cannot work, because elimination of the instability wouldstill allow rapid splicing to outrace Rev-export (Figure 1,C and 1D). Nevertheless, though parsimony does notrequire more than export to be involved in Rev over-coming CRS/INS inhibition and promoting cytoplasmicexpression of unspliced mRNA, there is nothing to saythat a multifunctional protein such as Rev does not alsoget directly involved in prying mRNA from variousinteracting partners which would otherwise contributeto its retention, such as components of aberrant splicingcomplexes. How MATR3 fits into any of these scenariosremains to be determined.Finally, MATR3 has also been identified as interactingwith the molecular chaperone cluster implicated bysiRNA screening to be involved in viral assembly [17].This could underlie observations that Rev is involved inencapsidation (see [18] and [2]).ConclusionsAs is generally the case, the answers to all of these ques-tions will emerge as more information is obtained con-cerning Rev/RRE and CRS/INS associated factors andtheir normal cellular roles. At the age of 24, the field ofRev remains rich and productive.Competing interestsThe author declares that they have no competing interests.Received: 10 July 2011 Accepted: 20 July 2011 Published: 20 July 2011References1. Rosen CA, Terwilliger E, Dayton A, Sodroski JG, Haseltine WA: Intrageniccis-acting art gene-responsive sequences of the humanimmunodeficiency virus. Proc Natl Acad Sci USA 1988, 85:2071-2075.2. Groom HC, Anderson EC, Lever AM: Rev: beyond nuclear export. J GenVirol 2009, 90:1303-1318.3. Suhasini M, Reddy TR: Cellular proteins and HIV-1 Rev function. Curr HIVRes 2009, 7:91-100.4. Cochrane AW, McNally MT, Mouland AJ: The retrovirus RNA traffickinggranule: from birth to maturity. Retrovirology 2006, 3:18.5. Yedavalli VSRK, Jang K-T: Matrin 3 is a co-factor for HIV-1 Rev inregulating post-transcriptional viral gene expression. Retrovirology 2011,8:61.6. Kula A, Guerra J, Knezevich A, Kleva D, Michael D, Myers P, Marcello A:Characterization of the HIV-1 RNA associated proteome identifies Matrin3 as a nuclear cofactor of Rev function. Retrovirology 2011, 8:60.7. Zolotukhin AS, Michalowski D, Bear J, Smulevitch SV, Traish AM, Peng R,Patton J, Shatsky IN, Felber BK: PSF acts through the humanimmunodeficiency virus type 1 mRNA instability elements to regulatevirus expression. Mol Cell Biol 2003, 23:6618-6630.8. Belgrader P, Dey R, Berezney R: Molecular cloning of matrin 3. A 125-kilodalton protein of the nuclear matrix contains an extensive acidicdomain. J Biol Chem 1991, 266:9893-9899.9. Nakayasu H, Berezney R: Nuclear matrins: identification of the majornuclear matrix proteins. Proc Natl Acad Sci USA 1991, 88:10312-10316.10. Hisada-Ishii S, Ebihara M, Kobayashi N, Kitagawa Y: Bipartite nuclearlocalization signal of matrin 3 is essential for vertebrate cells. BiochemBiophys Res Commun 2007, 354:72-76.11. Zeitz MJ, Malyavantham KS, Seifert B, Berezney R: Matrin 3: chromosomaldistribution and protein interactions. J Cell Biochem 2009, 108:125-133.12. Zhang Z, Carmichael GG: The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs. Cell 2001, 106:465-475.13. Shav-Tal Y, Zipori D: PSF and p54(nrb)/NonO–multi-functional nuclearproteins. FEBS Lett 2002, 531:109-114.14. Kameoka S, Duque P, Konarska MM: p54(nrb) associates with the 5’ splicesite within large transcription/splicing complexes. Embo J 2004,23:1782-1791.15. Buxade M, Morrice N, Krebs DL, Proud CG: The PSF.p54nrb complex is anovel Mnk substrate that binds the mRNA for tumor necrosis factoralpha. J Biol Chem 2008, 283:57-65.16. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ: Proteomicanalysis of the mammalian nuclear pore complex. J Cell Biol 2002,158:915-927.17. Bushman FD, Malani N, Fernandes J, D’Orso I, Cagney G, Diamond TL,Zhou H, Hazuda DJ, Espeseth AS, Konig R, et al: Host cell factors in HIVreplication: meta-analysis of genome-wide studies. PLoS Pathog 2009, 5:e1000437.18. Cockrell AS, van Praag H, Santistevan N, Ma H, Kafri T: The HIV-1 Rev/RREsystem is required for HIV-1 5’ UTR cis elements to augmentencapsidation of heterologous RNA into HIV-1 viral particles.Retrovirology 2011, 8:51.doi:10.1186/1742-4690-8-62Cite this article as: Dayton: Matrin 3 and HIV Rev Regulation of mRNA.Retrovirology 2011 8:62.Submit your next manuscript to BioMed Centraland take full advantage of: • Convenient online submission• Thorough peer review• No space constraints or color figure charges• Immediate publication on acceptance• Inclusion in PubMed, CAS, Scopus and Google Scholar• Research which is freely available for redistributionSubmit your manuscript at www.biomedcentral.com/submitDayton Retrovirology 2011, 8:62http://www.retrovirology.com/content/8/1/62Page 3 of 3

A: Characterization of the HIV-1 RNA associated proteome identifies Matrin 3 as a nuclear cofactor of Rev function. Retrovirology

al: Host cell factors in HIV replication: meta-analysis of genome-wide studies. PLoS Pathog

AM: Rev: beyond nuclear export.

Bipartite nuclear localization signal of matrin 3 is essential for vertebrate cells. Biochem Biophys Res Commun

BK: PSF acts through the human immunodeficiency virus type 1 mRNA instability elements to regulate virus expression. Mol Cell Biol

CG: The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha.

GG: The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously Ato-I edited RNAs. Cell

Intragenic cis-acting art gene-responsive sequences of the human immunodeficiency virus.

Jang K-T: Matrin 3 is a co-factor for HIV-1 Rev in regulating post-transcriptional viral gene expression. Retrovirology

Konarska MM: p54(nrb) associates with the 5’ splice site within large transcription/splicing complexes. Embo J

Matrin 3: chromosomal distribution and protein interactions.

Matunis MJ: Proteomic analysis of the mammalian nuclear pore complex.

Molecular cloning of matrin 3. A 125-kilodalton protein of the nuclear matrix contains an extensive acidic domain.

Mouland AJ: The retrovirus RNA trafficking granule: from birth to maturity. Retrovirology

Nuclear matrins: identification of the major nuclear matrix proteins.

Reddy TR: Cellular proteins and HIV-1 Rev function. Curr HIV Res

Zipori D: PSF and p54(nrb)/NonO–multi-functional nuclear proteins.

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