A novel type of FKBP in the secretory pathway of Neurospora crassa |
| |
Authors: | Solscheid B Tropschug M |
| |
Affiliation: | Institute für Biochemie und Molekularbiologie der Universit?t Freiburg, Germany. |
| |
Abstract: | FKBPs define a subfamily of peptidyl-prolyl cis/trans isomerases (PPIases). PPIases are known to play roles in cellular protein folding, protein interactions and signal transduction. Here we describe NcFKBP22 from Neurospora crassa, a novel type of FKBP. NcFKBP22 is synthesized as a precursor protein with a cleavable signal sequence. In addition to a typical FKBP domain in the amino-terminal part mature NcFKBP22 contains a novel second domain which is unique amongst all known FKBPs. The amino acid composition of this carboxy-terminal domain is highly biased. Secondary structure predictions suggest that this domain may form an amphipathic -helix. The carboxy-terminus of NcFKBP22 is –HNEL, a potential endoplasmic reticulum (ER) retention signal, suggesting that NcFKBP22 is a resident protein of the ER. |
| |
Keywords: | Prolyl isomerase FKBP Endoplasmic reticulum Late embryogenesis abundant protein Protein folding |
本文献已被 ScienceDirect PubMed 等数据库收录! |