Abstract
JARID1B (jumonji AT rich interactive domain 1B) is a large nuclear protein that is highly expressed in breast cancers and is proposed to function as a repressor of gene expression. In this paper, a phage display screen using the N-terminus of JARID1B as bait identified one of the JARID1B interacting proteins, namely PcG protein (Polycomb group) hPc2. We demonstrated that the C-terminal region, including the COOH box, was required for the interaction with the N-terminus of JARID1B. In a reporter assay system, co-expression of JARID1B with hPc2 significantly enhanced the transcriptional repression. These results support a role for hPc2 acting as a transcriptional co-repressor.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Cell Line, Tumor
-
DNA-Binding Proteins / chemistry*
-
DNA-Binding Proteins / metabolism*
-
Humans
-
Jumonji Domain-Containing Histone Demethylases
-
Ligases
-
Nuclear Proteins / chemistry*
-
Nuclear Proteins / metabolism*
-
Oxidoreductases, N-Demethylating / chemistry*
-
Oxidoreductases, N-Demethylating / metabolism*
-
Peptide Library
-
Polycomb-Group Proteins
-
Protein Binding
-
Repressor Proteins / chemistry
-
Repressor Proteins / metabolism*
-
Transcription, Genetic*
-
Ubiquitin-Protein Ligases
Substances
-
DNA-Binding Proteins
-
Nuclear Proteins
-
Peptide Library
-
Polycomb-Group Proteins
-
Repressor Proteins
-
Jumonji Domain-Containing Histone Demethylases
-
KDM5B protein, human
-
Oxidoreductases, N-Demethylating
-
Ubiquitin-Protein Ligases
-
Ligases
-
CBX4 protein, human