HSP60 — Neurospora crassa

Summary

NCU01589, designated HSP60 in Neurospora crassa on chromosome 2, encodes a chaperonin of the Cpn60/GroEL family with ATP-dependent protein folding chaperone activity, ATP hydrolase activity, and the ability to bind host cell surfaces, integrins, DNA replication origins, single-stranded DNA, and other chaperone proteins. The gene is associated with protein denaturation, de novo protein folding, refolding, stabilization, chaperone-mediated protein complex assembly, protein import into mitochondria and the mitochondrial intermembrane space, mitochondrial matrix protein import, protein secretion, activation of the cellular response to heat stress, the mitochondrial unfolded protein response, response to heat and stress generally, cellulose breakdown, and cellular osmotic response. It localizes to mitochondria, the mitochondrial inner membrane, lumen, envelope lumen, and nucleoid, the cytoplasm, the fungal-type cell wall, the TriC complex, and the post-mRNA release spliceosomal complex. Phenotypic associations include abnormal colony shape, cytoskeleton morphology, and mitochondrial distribution; decreased mitochondrial transport, cytokinesis, and prion inheritance; increased mitochondrial rho- mutation frequency and silencing; and absent anaerobic growth, pexophagy, and mitochondrial genome maintenance. Related genes in other species link the family to protein content.