Review
Version 1
Preserved in Portico This version is not peer-reviewed
Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms
Version 1
: Received: 25 October 2018 / Approved: 26 October 2018 / Online: 26 October 2018 (05:20:51 CEST)
A peer-reviewed article of this Preprint also exists.
Barik, S. Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms. Biomolecules 2018, 8, 148. Barik, S. Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms. Biomolecules 2018, 8, 148.
Abstract
The dual-family peptidylprolyl cis-trans isomerases (immunophilins) represent naturally occurring chimera of classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker, and are found exclusively in monocellular organisms. The modular builds of these molecules represent two distinct types: CYN-(linker)-FKBP and FKBP-3TPR-CYN. Abbreviated respectively as CFBP and FCBP, the two classes also exhibit distinct organism preference, the CFBP being found in prokaryotes, and FCBP, in eukaryotes. This review summarizes the mystery of these unique class of prolyl isomerases, focusing on their host organisms, potential physiological role, and likely routes of evolution.
Keywords
peptidylprolyl isomerase; chaperone; immunophilin; extremophile; intrinsic disorder
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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