Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two mammalian representatives in a family of phylogenetically conserved proteins with a role in the biogenesis of Fe/S proteins
| Autor: | Yann Lécluse, Christine Scamps, Marie-Geneviève Mattei, Stéphanie Lorain, Marc Lipinski |
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| Rok vydání: | 2001 |
| Předmět: |
Iron-Sulfur Proteins
DNA Complementary Protein family EMX2 Molecular Sequence Data Biophysics Cell Cycle Proteins Biology In Vitro Techniques Biochemistry Conserved sequence Mice Structural Biology Sequence Homology Nucleic Acid Two-Hybrid System Techniques HSPA2 Genetics Animals Humans Histone Chaperones Amino Acid Sequence Nuclear protein Conserved Sequence In Situ Hybridization Phylogeny HSPA9 Base Sequence Sequence Homology Amino Acid Chromosome Mapping Nuclear Proteins Small acidic protein Chromosomal region Carrier Proteins HeLa Cells Transcription Factors |
| Zdroj: | Biochimica et biophysica acta. 1517(3) |
| ISSN: | 0006-3002 |
| Popis: | The human HIRA protein is encoded from a region of chromosome 22q that is critical for the DiGeorge syndrome and the velocardiofacial syndrome. We have previously reported that it directly interacts with core histones, with a novel histone-binding protein, HIRIP3, and during mouse embryogenesis, with the developmentally regulated homeodomain protein Pax3, suggesting a promoter-targeted function at the chromatin level. We here report on HIRA-interacting protein 5 (HIRIP5), a small acidic protein that interacted with HIRA in a double-hybrid screen performed in yeast and in in vitro protein interaction experiments. HIRIP5 has highly conserved homologs in both prokaryotes and eukaryotes, including the NFU1 gene product which has been implicated in iron metabolism in mitochondria of the yeast Saccharomyces cerevisiae. By radioactive in situ hybridization, the HIRIP5 gene was mapped to the 2p13-p15 chromosomal region, separate from any region previously associated with DiGeorge syndrome. |
| Databáze: | OpenAIRE |
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