PUBLICATION
Characterization of hrg22, a human homologue of the putative tumor suppressor gene hic1
- Authors
- Deltour, S., Pinte, S., Guerardel, C., and Leprince, D.
- ID
- ZDB-PUB-010918-7
- Date
- 2001
- Source
- Biochemical and Biophysical Research Communications 287(2): 427-434 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- Carrier Proteins/genetics*
- Cell Nucleus/metabolism
- Chromosome Mapping
- Chromosomes, Human, Pair 22*
- Conserved Sequence
- DNA-Binding Proteins*
- Gene Expression/drug effects
- Genes, Tumor Suppressor/genetics*
- Genome, Human
- Humans
- Hydroxamic Acids/pharmacology
- Kruppel-Like Transcription Factors
- Molecular Sequence Data
- Protein Structure, Tertiary
- Sequence Homology, Amino Acid
- Transcription Factors/chemistry
- Transcription Factors/genetics*
- Tumor Suppressor Proteins*
- Zebrafish
- Zebrafish Proteins
- PubMed
- 11554746 Full text @ Biochem. Biophys. Res. Commun.
Citation
Deltour, S., Pinte, S., Guerardel, C., and Leprince, D. (2001) Characterization of hrg22, a human homologue of the putative tumor suppressor gene hic1. Biochemical and Biophysical Research Communications. 287(2):427-434.
Abstract
Database searches identified on chromosome 22q11.2, a region subject to translocations, an homologue of the HIC1 (hypermethylated in cancer) candidate tumor suppressor gene located at 17p13.3. This gene was termed HRG22 for HIC1-related gene on chromosome 22. We have characterized a new HRG22 upstream coding exon and defined the complete coding sequence of the human and zebrafish HRG22 genes. Alignment of the HRG22 and HIC1 proteins from various species revealed high sequence homology in their N-terminal BTB/POZ and five C-terminal C(2)H(2) zinc finger domains and highlighted a conserved GLDLSKK/R peptide in their middle region. The full-length HRG22 and HIC1 proteins colocalize onto nuclear dots and share several functional properties since their BTB/POZ domains heterodimerize and are autonomous transcriptional repression domain insensitive to Trichostatin A, a histone deacetylase (HDAC) inhibitor. Thus, HIC1 and HRG22 define a subgroup of BTB/POZ domains unable to recruit repressing complexes containing an HDAC activity.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping