1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids.
The small heat-shock proteins (Hsps) exist as large aggregates and function by interacting and stabilising non-native proteins in a chaperone-like manner. Two-dimensional 1H NMR spectroscopy of mouse Hsp25 reveals that the last 18 amino acids have great flexibility with motion that is essentially independent of the domain core of the protein. The lens protein, alpha-crystallin, is homologous to Hsp25 and its two subunits also have flexible C-terminal extensions. The flexible region in Hsp25 encompasses exactly that expected from sequence comparison with alpha-crystallin implying that both proteins have similar structures and that the C-terminal extensions could be of functional importance for both proteins.
Carver
J A
JA
Australian Cataract Research Foundation, Department of Chemistry, University of Wollongong, NSW, Australia.
Esposito
G
G
Schwedersky
G
G
Gaestel
M
M
D000595:Amino Acid Sequence; D000818:Animals; D003459:Crystallins / Q000737:chemistry; D006360:Heat-Shock Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D003459:Crystallins; D006360:Heat-Shock Proteins; C486113:Hsbp1 protein, mouse; D018832:Molecular Chaperones; D009363:Neoplasm Proteins