MSI3 — Aspergillus fumigatus

Summary

AFU1G12610 (AfMSI3, also known as AfHSP88) encodes an Hsp70 chaperone family protein with holdase activity, adenyl-nucleotide exchange factor activity, and protein translocase activity. It is associated with protein folding and refolding, the ER-associated degradation (ERAD) pathway, the unfolded protein response (UPR), and SRP-dependent and posttranslational protein targeting and translocation to the ER. The gene is linked to fungal-type cell wall beta-glucan biosynthesis, cellular responses to farnesol and osmotic stress, and karyogamy during conjugation. Localization evidence places the product in the ER lumen and chaperone complex, the plasma membrane, cytoplasm, nucleus, and fungal biofilm matrix. Phenotypic associations include increased thermotolerance, altered cell cycle progression (particularly G2/M and anaphase), abnormal spore germination, increased adhesion, premature apoptosis, and altered prion inheritance. Related genes in other species link the family to oxidative stress response and protein content.