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J Biol Chem, Vol. 275, Issue 7, 4848-4857, February 18, 2000
From the Regulation of viral genome expression is the
result of complex cooperation between viral proteins and host cell
factors. We report here the characterization of a novel cellular factor
sharing homology with the specific cysteine-rich C-terminal domain of the basic helix-loop-helix repressor protein I-mfa. The synthesis of
this new factor, called HIC for Human I-mfa
domain-Containing protein, is controlled at the
translational level by two different codons, an ATG and an upstream
non-ATG translational initiator, allowing the production of two protein
isoforms, p32 and p40, respectively. We show that the HIC protein
isoforms present different subcellular localizations, p32 being mainly
distributed throughout the cytoplasm, whereas p40 is targeted to the
nucleolus. Moreover, in trying to understand the function of HIC, we
have found that both isoforms stimulate in T-cells the expression of a
luciferase reporter gene driven by the human T-cell leukemia virus type
I-long terminal repeat in the presence of the viral transactivator Tax. We demonstrate by mutagenesis that the I-mfa-like domain of HIC is
involved in this regulation. Finally, we also show that HIC is able to
down-regulate the luciferase expression from the human immunodeficiency
virus type 1-long terminal repeat induced by the viral transactivator
Tat. From these results, we propose that HIC and I-mfa represent two
members of a new family of proteins regulating gene expression and
characterized by a particular cysteine-rich C-terminal domain.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF054589.
Molecular Cloning of a Novel Human I-mfa Domain-containing
Protein That Differently Regulates Human T-cell Leukemia Virus Type
I and HIV-1 Expression*
§,¶,
,, and**
Institut de Biologie, Laboratoire Infections
Rétrovirales et Signalisation Cellulaire,
CRBM-CNRS UPR 1086, 4 Boulevard Henri IV,
34060 Montpellier, France
*
This work was supported in part by institutional grants from
the CNRS and by Association pour la Recherche sur le Cancer Grant 6238.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Biochemistry and Molecular Biology,
Colorado State University, Fort Collins, CO 80523-1870.
**
To whom correspondence should be addressed: Laboratoire
Infections Rétrovirales et Signalisation Cellulaire, Institut de Biologie, 4 Bd. Henri IV, 34060 Montpellier, France. Tel.: (33) 4 67 60 86 60; Fax: (33) 4 67 60 44 20; E-mail:
mesnard@crbm.cnrs-mop.fr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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