Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c
| Autor: | Donald G. Payan, Kirk J. Hayenga, Joseph Fisher, Bruce B. Wang |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Recombinant Fusion Proteins
Blotting Western Molecular Sequence Data Fluorescent Antibody Technique Gene Expression Saccharomyces cerevisiae Biology Biochemistry Cell Line Cyclophilins Complementary DNA Animals Humans Amino Acid Sequence Lymphocytes Cloning Molecular Tyrosine Molecular Biology Peptide sequence Serpins Cyclophilin Amino Acid Isomerases Gene Library Cell Nucleus Messenger RNA Base Sequence Sequence Homology Amino Acid Proteins Cell Biology Transfection Peptidylprolyl Isomerase Subcellular localization Immunohistochemistry Molecular biology Cell culture Carrier Proteins Research Article |
| Zdroj: | Biochemical Journal. 314:313-319 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3140313 |
| Popis: | We have identified a novel human cyclophilin (hCyP-60) which interacts with the proteinase inhibitor eglin c using the yeast two-hybrid system. A cDNA isolated from a Raji B lymphocyte library reveals a domain showing sequence similarity to known cyclophilins flanked by unique N- and C-terminal residues. In addition, hCyP-60 contains a tyrosine residue (Tyr389) instead of a tryptophan residue found in most eukaryotic cyclophilins at a position important for cyclosporin binding. Northern and Western analysis reveal widespread expression with considerable tissue-specific variation. Specifically, the highest levels of mRNA are detected in the thymus, pancreas, testis, and K-562 cell line, while the most protein is detected in the kidney. Immunohistochemistry indicates a nuclear-specific localization both in transfected cells and tissue sections. hCyP-60's specific subcellular localization and conserved amino acid sequence suggest that it may play a specific role in the nucleus. |
| Databáze: | OpenAIRE |
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