Nucleic Acids Research, Vol 24, Issue 10 1855-1864, Copyright © 1996 by Oxford University Press
IM Clauss, M Chu, JL Zhao and LH Glimcher
The transcription factor hXBP-1 belongs to the family of basic
region/leucine zipper (bZIP) proteins and interacts with the cAMP
responsive element (CRE) of the major histocompatibility complex (MHC)
class II A alpha, DR alpha and DP beta genes. However, the developmental
expression of hXBP-1 as revealed by in situ hybridization in mouse embryos,
has suggested that it interacts with the promoter of additional genes. To
identify other potential target genes of this factor, we performed binding
site selection experiments with recombinant hXBP-1 protein. The results
indicated that hXBP-1 binds preferably to the CRE-like element
GAT-GACGTG(T/G)NNN(A/T)T, wherein the core sequence ACGT is highly
conserved, and that it also binds to some TPA response elements (TRE).
hXBP-1 can transactivate multimers of the target sequences to which it
binds in COS cells, and the level of transactivation directly correlates
with the extent of binding as observed in gel retardation experiments. One
target sequence that is strongly bound by hXBP-1 is the 21 bp repeat in the
HTLV-1 LTR, and we demonstrate here that hXBP-1 can transactivate the
HTLV-1 LTR. Further, the transactivation domain of hXBP-1 encompasses a
large C-terminal region of the protein, containing domains rich in
glutamine, serine and threonine, and proline and glutamine residues, as
shown in transient transfection experiments using hXBP-1-GAL4 fusion
proteins and a reporter gene under the control of GAL4-binding sites.
ARTICLES
The basic domain/leucine zipper protein hXBP-1 preferentially binds to and transactivates CRE-like sequences containing an ACGT core
Department of Cancer Biology, Harvard School of Public Health, Boston, MA 02115-6023, USA.
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