Biochemical Analysis of a Cytosolic Small Heat Shock Protein, NtHSP18.3, from Nicotiana tabacum

• Published in: Molecules and cells 2005-06, Vol.19 (3), p.328-333
• Main Authors: Yu, J.H. (Seoul National University, Seoul, Republic of Korea), Kim, K.P. (Seoul National University, Seoul, Republic of Korea), Park, S.M. (Seoul National University, Seoul, Republic of Korea), Hong, C.B. (Seoul National University, Seoul, Republic of Korea), E-mail: [e-mail]
• Format: Article
• Language: English
• Subjects: Anilino Naphthalenesulfonates - metabolism; Citrate (si)-Synthase - drug effects; Cloning, Molecular; Cytosol - chemistry; Escherichia coli - metabolism; Escherichia coli Proteins - drug effects; Heat-Shock Proteins - isolation & purification; Heat-Shock Proteins - physiology; Hot Temperature; IN VITRO; In Vitro Activity; Luciferases - drug effects; Molecular Chaperones; Molecular Chaperones - physiology; Nicotiana - chemistry; Nicotiana - genetics; Protein Denaturation - drug effects; Small Heat Shock Proteins; Temperature Stress
• ISSN: 1016-8478
• DOI: 10.1016/S1016-8478(23)13176-1

Small heat shock proteins (sHSPs) are widely distributed, and their function and diversity of structure have been much studied in the field of molecular chaperones. In plants, which frequently have to cope with hostile environments, sHSPs are much more abundant and diverse than in other forms of life. In response to high temperature stress, sHSPs of more than twenty kinds can make up more than 1% of soluble plant proteins. We isolated a genomic clone, NtHSP18.3, from Nicotiana tabacum that encodes the complete open reading frame of a cytosolic class I small heat shock protein. To investigate the function of NtHSP18.3 in vitro, it was overproduced in Escherichia coli and purified. The purified NtHSP18.3 had typical molecular chaperone activity as it protected citrate synthase and luciferase from high temperature-induced aggregation.