Structure and expression of major histocompatibility complex-binding protein 2, a 275-kDa zinc finger protein that binds to an enhancer of major histocompatibility complex class I genes
Publication date
1992
Authors
Veer, L.J. van 't
Lutz, P.M.
Isselbacher, K.J.
Bernards, R.A.
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Article
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Abstract
We have isolated a cDNA encoding a transcription
factor that binds to the enhancer of major histocompatibility
complex (MHC) class I genes. MHC-binding protein 2
(MBP-2) is a 275-kDa protein, containing two sets of widely
separated zinc fingers and a stretch of highly acidic amino acids,
a putative transactivation domain. The two zinc ringer regions,
when expressed individually as bacterial fusion proteins, bind
with highest affinity to the MHC class I gene enhancer. Several
proteins found in mammalian nuclear extracts bind the MHC
class I enhancer in an electrophoresis mobility shift assay. Only
one of these, a ubiquitously expressed factor, forming a slowmigrating
retarded complex, can be supershifted by a MBP-2
antiserum. The same antiserum also precipitates a protein of
>250 kDa from COS cells transfected with a MBP-2 expression
vector. Our data indicate that MBP-2 is a transcription factor
involved in the regulation of MHC class I gene expression.