Identification of all FK506-binding proteins from Neurospora crassa
| Autor: | Margarida Duarte, Arnaldo Videira, Susana Soares, Maximilian Tropschug, Débora Pinto |
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| Rok vydání: | 2008 |
| Předmět: |
Cytoplasm
Isomerase activity Green Fluorescent Proteins Endoplasmic Reticulum Microbiology Neurospora crassa Fungal Proteins Tacrolimus Binding Proteins Immunophilins Genes Reporter Genetics Cell Nucleus biology Endoplasmic reticulum fungi Crassa biology.organism_classification Mitochondria FKBP Biochemistry Microscopy Fluorescence Chaperone (protein) biology.protein Gene Deletion |
| Zdroj: | Fungal genetics and biology : FGB. 45(12) |
| ISSN: | 1096-0937 |
| Popis: | Immunophilins are intracellular receptors of immunosuppressive drugs, carrying peptidyl-prolyl cis-trans isomerase activity, with a general role in protein folding but also involved in specific regulatory mechanisms. Four immunophilins of the FKBP-type (FK506-binding proteins) were identified in the genome of Neurospora crassa. Previously, FKBP22 has been located in the endoplasmic reticulum as part of chaperone/folding complexes and FKBP13 has been found to have a dual location in the cytoplasm and mitochondria. FKBP11 is apparently located exclusively in the cytoplasm. It is not expressed during vegetative development of the fungus although its expression can be induced with calcium and during sexual development. Overexpression of the respective gene appears to confer a growth advantage to the fungus in media containing some divalent ions. FKBP50 is a nuclear protein and its genetic inactivation leads to a temperature-sensitive phenotype. None of these proteins is, alone or in combination, essential for N. crassa, as demonstrated by the isolation of a mutant strain lacking all four FKBPs. |
| Databáze: | OpenAIRE |
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