Journal of Biotechnology & Biomaterials
Open Access

Abstract

Cyclophilin (CYPs) and FKBPs are abundant and ubiquitous proteins belonging to familyof peptidyl-prolylcis/trans isomerase (PPIase) which regulate much metabolism through an isomerization of proline residues during protein folding and chaperons. They are collectively referred to as Immunophilin (IMMs). They are highly conserved in all organisms. IMMs geneCYP and FKBP in phytopathogenic fungi L. maculanswere identified and classified and thus given the appropriate name for each IMM considering the Hidden Morkov Model (HMM) score. There were 12 CYPs and 5 FKBPs identified. Furthermore, the putative identified genes were characterized based on domain architecture, chromosomal distribution, sequence alignment, phylogentic analysis, seondary structure, gene structure, and GO terms. Domain architecture analysis revealed the presence of conserved catalytic Cyclophilin-like domain (CLD) in CYP and FK506 binding domain and other additional domains. Sub-cellular localization analysis showed that IMM are mainly present in cytoplasm, nucleus and mitochondria however, lacks chroloplast and ER. GO analysis predict their significant role in protein folding and PPIase activity. Gene structure analysis indicates that introns are shorter than exons due to its compact genome. Classification of the putative CYPs and FKBPs in phytopathogenic fungi L. maculans provides the information about their functional significance.

Biography

Kamal Sharma has completed his PhD from the Central Tuber Crops Research Institute, Trivandrum, India. At present he is doing his postdoctoral at Genetics and Breeding Department, Czech University of Life Science, Prague. He is studying sequential polymorphisms of self-incompatibility locus (S-locus) in cultivated and wild cherries (Prunusavium L.). He has published 24 research papers and abstracts at different conferences.