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Full-Text Articles in Physical Sciences and Mathematics
Small Heat Shock Protein Activity Is Regulated By Variable Oligomeric Substructure, J. L. Benesch, M. Ayoub, C. V. Robinson, J. A. Aquilina
Small Heat Shock Protein Activity Is Regulated By Variable Oligomeric Substructure, J. L. Benesch, M. Ayoub, C. V. Robinson, J. A. Aquilina
J. A. Aquilina
The alpha-crystallins are members of the small heat shock protein (sHSP) family of molecular chaperones which have evolved to minimize intracellular protein aggregation, however they are also implicated in a number of protein deposition diseases. In this study we have employed novel mass spectrometry techniques to investigate the changes in quaternary structure associated with this switch from chaperone to adjuvant of aggregation. We have replicated the oligomeric rearrangements observed for in vivo disease-related modifications, without altering the protein sequence, by refolding the alpha-crystallins in vitro. This refolding results in a loss of dimeric substructure concomitant with an augmentation of substrate …
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
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, …