A P39R mutation at the N-terminal domain of human alpha B-crystallin regulates its oligomeric state and chaperone-like activity

作者：Numoto Nobutaka; Kita Akiko^*; Fujii Noriko; Miki Kunio

来源：Biochemical and Biophysical Research Communications, 2012, 425(3): 601-606.

DOI：10.1016/j.bbrc.2012.07.138

• Small heat shock protein
• Molecular chaperone
• Quaternary assembly
• Protein aggregation
• Secondary structure
• Cataract

Recent structure analyses of alpha B-crystallin have proposed some models of the N-terminal domain and the manner of oligomerization, whereas the effects of the significantly high content of Pro residues at the N-terminal domain remain unclear. We report the properties of a novel P39R mutant of alpha B-crystallin. The content of alpha-helix was increased, and the molecular size of the P39R mutant was larger than that of wild-type alpha B-crystallin. A slight loss of chaperone-like activity was observed using alcohol dehydrogenase (ADH), while a significant increase was detected by insulin assay. The Pro residue at the N-terminal domain of alpha B-crystallin is important for oligomerization and function.

• 出版日期2012-8-31