Pinto Débora, Duarte Margarida, Soares Susana, Tropschug Maximilian, Videira Arnaldo
IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal.
Fungal Genet Biol. 2008 Dec;45(12):1600-7. doi: 10.1016/j.fgb.2008.09.011. Epub 2008 Oct 10.
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.
免疫亲和蛋白是免疫抑制药物的细胞内受体，具有肽基脯氨酰顺反异构酶活性，在蛋白质折叠中起普遍作用，但也参与特定的调节机制。在粗糙脉孢菌的基因组中鉴定出了四种FKBP型免疫亲和蛋白（FK506结合蛋白）。此前，FKBP22作为伴侣/折叠复合物的一部分定位于内质网，而FKBP13在细胞质和线粒体中都有定位。FKBP11显然仅定位于细胞质。在真菌的营养生长过程中它不表达，不过其表达可在有钙存在时以及有性发育过程中被诱导。各自基因的过表达似乎赋予真菌在含有某些二价离子的培养基中生长的优势。FKBP50是一种核蛋白，其基因失活会导致温度敏感型表型。如通过分离出缺失所有四种FKBP的突变菌株所证明的，这些蛋白单独或组合起来对粗糙脉孢菌都不是必需的。
