Plant immunophilins: a review of their structure-function relationship

Area of Science:

• Plant biology
• Molecular chaperones
• Protein folding

Background:

• Immunophilins, including FK506 binding proteins (FKBPs) and cyclophilins (CYPs), are crucial for protein folding across all life forms.
• While sharing functions as peptidyl prolyl isomerases, FKBPs and CYPs have diverse sequences and structures.
• These proteins are found in various organisms, from viruses to plants and animals.

Purpose of the Study:

• To review the structural and functional diversity of plant FKBP and cyclophilin families.
• To highlight novel functions and structural properties of plant immunophilins beyond protein folding.
• To stimulate further research into plant immunophilins and their roles in plant biology.

Main Methods:

• Literature review focusing on structural and functional studies of plant immunophilins.
• Analysis of sequence, structure, and subcellular localization data for FKBPs and CYPs.
• Synthesis of current knowledge on plant immunophilin diversity and functions.

Main Results:

• Plant immunophilins display significant structural and functional diversity, extending beyond their roles as peptidyl prolyl isomerases.
• Subcellular localization, particularly in the thylakoid lumen, suggests unique roles in plant-specific processes.
• Despite their importance, comprehensive structural and functional data for plant immunophilins remain limited.

Conclusions:

• The diversity in sequence, structure, and localization contributes to the varied roles of plant immunophilins as molecular chaperones.
• Plant immunophilins in the thylakoid lumen offer potential insights into photosynthesis regulation.
• Further structural and functional investigations are essential to fully understand the significance of plant immunophilins in plant biology.