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J. Biol. Chem., Vol. 276, Issue 49, 46445-46452, December 7, 2001
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From the Departments of Medicine and Molecular & Cellular Biology,
Baylor College of Medicine, Houston, Texas 77030
Mammalian homologues of DnaJ proteins, also known
as Hsp40 proteins, are co-chaperonins that complement Hsp70 chaperone
function. Using the yeast two-hybrid system, we cloned an
apolipoprotein (apo) B mRNA editing complementation protein, called
apobec-1-binding protein-2 (ABBP-2), and found that it is a Class II
DnaJ homologue. ABBP-2 binds to apobec-1, the mammalian apoB mRNA
editase, via its J domain and neighboring G/F domain. It is a
ubiquitously expressed protein, and, by transfection analysis of
GFP-ABBP-2, we found that the protein is located in both the nucleus
and cytosol of transfected cells, with predominance in the nucleus.
Down-regulation of ABBP-2 expression in cultured cells inhibits
endogenous apobec-1-mediated apoB mRNA editing. Like other Hsp40
proteins, ABBP-2 binds to Hsp70 and has ATPase-stimulating activity.
Apobec-1-mediated apoB mRNA editing activity of in
vitro tissue extracts requires the presence of Hsp70/ABBP-2.
Although exogenously added ATP is not required for editing activity,
removal of the endogenous ATP present in these extracts, which disrupts
ABBP-2-Hsp70 interaction, completely inhibits editing. ABBP-2 differs
from previously described auxiliary proteins (ABBP-1, ACF, and GRY-RBP)
in that it does not contain any RNA recognition motifs. Not only is
ABBP-2 required for efficient apoB mRNA editing, this newly
discovered apobec-1-binding protein may help determine the subcellular
distribution and trafficking of apobec-1 via its interaction with the
chaperonin Hsp70.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AY054981.
A DnaJ Protein, Apobec-1-binding Protein-2, Modulates
Apolipoprotein B mRNA Editing*
*
This work was supported by National Institutes of Health
Grant HL-56668.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.
To whom correspondence should be addressed: Depts. of Medicine and
Molecular & Cellular Biology, Baylor College of Medicine, One Baylor
Plaza, Houston, TX 77030. Tel.: 713-798-4478; Fax: 713-798-8764;
E-mail: lchan@bcm.tmc.edu.
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