On. Denisenko et al., ZIK1, A TRANSCRIPTIONAL REPRESSOR THAT INTERACTS WITH THE HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN PARTICLE-K PROTEIN, The Journal of biological chemistry, 271(44), 1996, pp. 27701-27706
The heterogeneous nuclear ribonucleoprotein particle (hnRNP) K protein
is comprised of multiple modular domains that serve to engage a diver
se group of molecular partners including DNA, RNA, the product of the
proto-oncogene vav, and tyrosine and serine/threonine kinases. To iden
tify 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 positiv
e clones revealed a novel zinc finger protein, hereby denoted as Zik1.
In addition to the nine contiguous zinc fingers in the C terminus, Zi
k1 contains a KRAB-A domain thought to be involved in transcriptional
repression, Zik1 and K protein bound in vitro and co-immunoprecipitate
d from cell extracts indicating that in vivo their interaction is dire
ct. Expression of Gal4 DNA-binding domain-Zik1 fusion protein represse
d a gene promoter bearing Gal4-binding elements, indicating that from
cognate DNA elements Zik1 is a transcriptional repressor. The known di
verse nature of K protein molecular interactions and now the identific
ation of a K protein partner that is a transcriptional repressor lends
support to the notion that K protein is a remarkably versatile molecu
le that may be acting as a docking platform to facilitate communicatio
n among molecules involved in signal transduction and gene expression.