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(Received for publication, July 15, 1996)
From the The heterogeneous nuclear ribonucleoprotein
particle (hnRNP) K protein is comprised of multiple modular domains
that serve to engage a diverse group of molecular partners including
DNA, RNA, the product of the proto-oncogene vav, and
tyrosine and serine/threonine kinases. To identify additional K protein
molecular partners and to further understand its function, we used a
fragment of K protein as a bait in the yeast two-hybrid screen. The
deduced primary structure of one of the positive clones revealed a
novel zinc finger protein, hereby denoted as Zik1. In addition to the
nine contiguous zinc fingers in the C terminus, Zik1 contains a KRAB-A
domain thought to be involved in transcriptional repression. Zik1 and K
protein bound in vitro and co-immunoprecipitated from cell
extracts indicating that in vivo their interaction is
direct. Expression of Gal4 DNA-binding domain-Zik1 fusion protein
repressed a gene promoter bearing Gal4-binding elements, indicating
that from cognate DNA elements Zik1 is a transcriptional repressor. The
known diverse nature of K protein molecular interactions and now the
identification of a K protein partner that is a transcriptional
repressor lends support to the notion that K protein is a remarkably
versatile molecule that may be acting as a docking platform to
facilitate communication among molecules involved in signal
transduction and gene expression.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27701-27706
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,
,
and
Department of Medicine, University of
Washington, Seattle, Washington 98195 and the § Institute of
Protein Research, Puschino, Moscow Region 142292, Russia
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