Abstract
GCIP, a newly identified cyclin D-interacting protein, was found to reduce the phosphorylation of retinoblastoma protein and inhibit E2F1-mediated transcriptional activity. To explore more GCIP interacting proteins, the yeast two-hybrid screening using GCIP as a bait protein was performed. One novel gene, p29, was demonstrated to associate with GCIP in the yeast two-hybrid method and in vitro GST pull-down assay. Multiple tissue Northern blot analysis showed that p29 was abundantly expressed in the heart, skeletal muscle, and kidney relative to other tissues. The transient expression of HA-tagged p29 in HeLa cells localized in the nucleus. Taken together, we have isolated a novel protein, p29, which may be involved in the functional regulation of GCIP.
Copyright 2000 Academic Press.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Base Sequence
-
Cloning, Molecular
-
Cyclin D
-
Cyclins / metabolism
-
Glutathione Transferase / genetics
-
Humans
-
Molecular Sequence Data
-
Nuclear Proteins / chemistry
-
Nuclear Proteins / genetics*
-
Nuclear Proteins / metabolism*
-
Open Reading Frames
-
Protein Biosynthesis
-
RNA-Binding Proteins
-
Recombinant Fusion Proteins / metabolism
-
Recombinant Proteins / metabolism
-
Saccharomyces cerevisiae / genetics
-
Sequence Alignment
-
Sequence Homology, Amino Acid
-
Transcription Factors / genetics
-
Transcription Factors / metabolism*
Substances
-
CCNDBP1 protein, human
-
Cyclin D
-
Cyclins
-
GCIP-interacting protein p29, human
-
Nuclear Proteins
-
RNA-Binding Proteins
-
Recombinant Fusion Proteins
-
Recombinant Proteins
-
Transcription Factors
-
Glutathione Transferase