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Glutamic Acid Residues In The C-Terminal Extension Of Hsp25 Are Critical For Structural And Functional Integrity, A. M. Morris, T. M. Treweek, J. A. Aquilina, J. A. Carver, Mark J. Walker

J. A. Aquilina

Small heat shock proteins (sHsps) are intracellular molecular chaperones that prevent the aggregation and precipitation of partially-folded and destabilized proteins. sHsps are comprised of an evolutionarily conserved region of 80-100 amino acids denoted the α-crystallin domain which is flanked by regions of variable sequence and length: the N-terminal domain and the C-terminal extension. Whilst the two domains are known to be involved in organization of the quaternary structure of sHsps and interaction with their target proteins, the role of the C-terminal extension is enigmatic. Despite the lack of sequence similarity, the C-terminal extension of mammalian sHsps is typically a short, …