tailieunhanh - Báo cáo khoa học: Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity

Small heat shock proteins (sHsps) are intracellular molecular chaperones that prevent the aggregation and precipitation of partially folded and destabilized proteins. sHsps comprise an evolutionarily conserved region of 80–100 amino acids, denoted thea-crystallin domain, which is flanked by regions of variable sequence and length: the N-terminal domain and the C-terminal extension. | ỊFEBS Journal Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity Amie M. Morris1 Teresa M. Treweek2 J. A. Aquilina1 John A. Carver3 and Mark J. Walker1 1 Schoolof BiologicalSciences University of Wollongong Australia 2 Graduate Schoolof Medicine University of Wollongong Australia 3 Schoolof Chemistry Physics The University of Adelaide Australia Keywords C-terminalextension Hsp25 molecular chaperone protein aggregation small heat shock protein Correspondence M. J. Walker Schoolof BiologicalSciences University of Wollongong Wollongong NSW 2522 Australia Fax 61 2 4221 4135 Tel 61 2 4221 3439 E-mail mwalker@ J. A. Carver School of Chemistry Physics The University of Adelaide Adelaide SA 5005 Australia Fax 61 8 8303 4380 Tel 61 8 8303 3110 E-mail Received 19 February 2008 revised 14 September 2008 accepted 29 September 2008 doi Small heat shock proteins sHsps are intracellular molecular chaperones that prevent the aggregation and precipitation of partially folded and destabilized proteins. sHsps comprise an evolutionarily conserved region of 80-100 amino acids denoted the a-crystallin domain which is flanked by regions of variable sequence and length the N-terminal domain and the C-terminal extension. Although the two domains are known to be involved in the 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 polar segment which is unstructured and highly flexible and protrudes from the oligomeric structure. Both the polarity and flexibility of the C-terminal extension are important for the maintenance of sHsp solubility and for complexation with its target protein. In this study mutants of murine Hsp25 were prepared in which

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