Abstract

Plants have developed a variety of mechanisms and regulatory pathways to change their gene expression profiles in response to abiotic stress conditions and plant–microbe interactions. The plant–microbe interaction can be pathogenic or beneficial. Stress conditions, both abiotic and pathogenic, negatively affect the growth, development, yield and quality of plants, which is very important for crops. In contrast, the plant–microbe interaction could be growth-promoting. One of the proteins involved in plant response to stress conditions and plant–microbe interactions is cyclophilin. Cyclophilins (CyPs), together with FK506-binding proteins (FKBPs) and parvulins, belong to a big family of proteins with peptidyl-prolyl cis-trans isomerase activity (Enzyme Commission (EC) number 5.2.1.8). Genes coding for proteins with the CyP domain are widely expressed in all organisms examined, including bacteria, fungi, animals, and plants. Their different forms can be found in the cytoplasm, endoplasmic reticulum, nucleus, chloroplast, mitochondrion and in the phloem space. They are involved in numerous processes, such as protein folding, cellular signaling, mRNA processing, protein degradation and apoptosis. In the past few years, many new functions, and molecular mechanisms for cyclophilins have been discovered. In this review, we aim to summarize recent advances in cyclophilin research to improve our understanding of their biological functions in plant defense and symbiotic plant–microbe interactions.

Highlights

  • We aim to summarize recent advances in cyclophilin research to improve our understanding of their biological functions in plant defense and symbiotic plant–microbe interactions

  • Cyclophilins constitute a group of proteins with peptidyl-prolyl cis-trans isomerase activity (PPIase) involved in the folding of target proteins; they catalyze the reaction in both directions [1,2,3,4]

  • Various plant cyclophilins are encoded by numerous genes, revealing functional differentiation

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Summary

Introduction

Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Parvulins regulate the structure and function of eukaryotic RNA polymerase II catalyzing the cis-trans conversion of Ser5–Pro bonds within the carboxy–terminal domain (CTD) repeats, of the largest subunit of RNA polymerase II [9,10,11]. These three groups of proteins share little sequence homology but have in common the peptidyl–prolyl cis-trans isomerase activity involved in protein folding processes. It has been shown that some CyP transcripts accumulate in response to wounding, heat shock, and low temperature treatment as well as in symbiotic plant–microbe interactions [24,25,26,27,28]

Cyclophilin Domain Architecture
Cyclophilin Function in Abiotic Stress
Water Stress
Salinity Stress
Temperature Stress
Light Stress
Oxidative Stress
Other Stress Factors
Pathogenic Plant–Microbe Interactions
Beneficial Plant–Microbe Interactions
Conclusions
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