Heat shock response in Neurospora crassa: purification and some properties of HSP 80

• Published in: Biochemistry and cell biology Vol. 68; no. 10; pp. 1218 - 1221
• Main Authors: Roychowdhury, H.S, Kapoor, M
• Format: Journal Article
• Language: English
• Published: Canada 01.10.1990
• Subjects: characterization; Fungal Proteins - isolation & purification; glycoproteins; heat shock proteins; heat stress; Heat-Shock Proteins - isolation & purification; Heat-Shock Proteins - physiology; Hot Temperature; Molecular Weight; Neurospora crassa; Neurospora crassa - analysis; Neurospora crassa - physiology; purification; Structure-Activity Relationship
• DOI: 10.1139/o90-180
• ISSN: 0829-8211

The heat shock response of Neurospora crassa was investigated. A 80-kilodalton heat shock protein (HSP 80) was purified to near homogeneity from heat-shocked mycelial extracts employing ammonium sulphate fractionation, gel filtration, and ion-exchange and affinity chromatography. It was observed to migrate as a single band on one-dimensional sodium dodecyl sulphate--polyacrylamide gels, with a molecular mass of approximately 83 kilodaltons (kDa). On two-dimensional gels it resolved into four polypeptide species with isoelectric points in the acidic range, which on staining with periodic acid--Schiff method were demonstrated to be glycosylated. In the native state, HSP 80 had a molecular size of approximately 610 kDa.