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J Biol Chem, Vol. 273, Issue 29, 18220-18229, July 17, 1998
From the Laboratory of Gene Regulation, The Wheeler Institute for
Biomedical Research, Huntington, New York 11743
The transcription factor, NF-Y, plays a critical
role in tissue-specific major histocompatibility complex class II gene
transcription. In this report the biochemical properties of the
heterotrimeric NF-Y complex have been characterized during
stage-specific B-cell development, and in several class
II
Biochemical Characterization of the NF-Y Transcription Factor
Complex during B Lymphocyte Development
mutant B-cell lines, which represent distinct
bare lymphocyte syndrome class II genetic complementation groups. The
NF-Y complex derived from class II+ mature B-cells bound
with high affinity to anion exchangers, and eluted as an intact
trimeric complex, whereas, NF-Y derived from class II
plasma B-cells, and from bare lymphocyte syndrome group II cell lines,
RJ2.2.5 and RM3, dissociated into discrete NF-YA and NF-YB:C subunit
fractions. Recombination of the MPC11 plasma B-cell derived NF-Y A:B:C
complex with the low molecular mass protein fraction, NF-Y-associated factors (YAFs),
derived from mature A20 B-cell nuclei, conferred high affinity anion
exchange binding to NF-Y as an intact trimeric complex. Recombination
of the native NF-YA:B:C complex with the transcriptional cofactor, PC4,
likewise conferred high affinity NF-Y binding to anion exchangers, and
stabilized NF-Y interaction with CCAAT-box DNA motifs in
vitro. Interaction between PC4 and NF-Y was mapped to the
C-terminal region of PC4, and the subunit interaction subdomain of the
highly conserved DNA binding-subunit
interaction domain (DBD) of NF-YA. These results suggest
that in class II+ mature B-cells NF-Y is associated with
the protein cofactor, PC4, which may play an important role in
NF-Y-mediated transcriptional control of class II genes.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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