Abstract
The Krüppel-associated box A (KRAB-A) domain is an evolutionarily conserved transcriptional repressor domain present in approximately one-third of zinc finger proteins of the Cys2-His2 type. Using the yeast two-hybrid system, we report the isolation of a cDNA encoding a novel murine protein, KRAB-A interacting protein 1 (KRIP-1) that physically interacts with the KRAB-A region. KRIP-1 is a member of the RBCC subfamily of the RING finger, or Cys3HisCys4, family of zinc binding proteins whose other members are known to play important roles in differentiation, oncogenesis, and signal transduction. The KRIP-1 protein has high homology to TIF1, a putative modulator of ligand-dependent activation function of nuclear receptors. A 3.5-kb mRNA for KRIP-1 is ubiquitously expressed among all adult mouse tissues studied. When a GAL4-KRIP-1 fusion protein is expressed in COS cells with a chloramphenicol acetyltransferase reporter construct with five GAL4 binding sites, there is dose-dependent repression of transcription. Thus, KRIP-1 interacts with the KRAB-A region of C2H2 zinc finger proteins and may mediate or modulate KRAB-A transcriptional repressor activity.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
COS Cells
Conserved Sequence
Embryo, Mammalian
Gene Library
Kidney/metabolism
Mice
Molecular Sequence Data
Nuclear Proteins/biosynthesis,chemistry,metabolism
Recombinant Fusion Proteins/metabolism
Repressor Proteins/metabolism
Transcription Factors/biosynthesis,chemistry,metabolism
Transfection
Tripartite Motif-Containing Protein 28
Zinc Fingers
Chemicals
Nuclear Proteins
Recombinant Fusion Proteins
Repressor Proteins
Transcription Factors
Trim28 protein, mouse
Tripartite Motif-Containing Protein 28
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Kim S S
Renal Unit, Massachusetts General Hospital, Charlestown 02129, USA.
Chen Y M
O'Leary E
Witzgall R
Vidal M
Bonventre J V
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