摘要:Peptidyl-prolyl
cis–trans isomerases (PPIases) are the only class of enzymes capable of
cis–trans isomerization of the prolyl peptide bond. The PPIases, comprising of different families viz., cyclophilins, FK506-binding proteins (FKBPs), parvulins and protein phosphatase 2A phosphatase activators (PTPAs), play essential roles in different cellular processes. Though PPIase gene families have been characterized in different organisms, information regarding these proteins is lacking in
Penicillium species, which are commercially an important fungi group. In this study, we carried out genome-wide analysis of PPIases in different
Penicilliumspp
. and investigated their regulation by salt stress in a halotolerant strain of
Penicillium oxalicum. These analyses revealed that the number of genes encoding cyclophilins, FKBPs, parvulins and PTPAs in
Penicillium spp
. varies between 7–11, 2–5, 1–2, and 1–2, respectively. The halotolerant
P. oxalicum depicted significant enhancement in the mycelial PPIase activity in the presence of 15% NaCl, thus, highlighting the role of these enzymes in salt stress adaptation. The stress-induced increase in PPIase activity at 4 and 10 DAI in
P. oxalicum was associated with higher expression of
PoxCYP18. Characterization of PPIases in
Penicillium spp. will provide an important database for understanding their cellular functions and might facilitate their applications in industrial processes through biotechnological interventions.