Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Abstract Background Protein quality control mechanisms are essential for cell health and involve delivery of proteins to specific cellular compartments for recycling or degradation. In particular, stray hydrophobic proteins are captured in the aqueous cytosol by a co-chaperone, the small glutamine-r...

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Main Authors: Santiago Martínez-Lumbreras, Ewelina M. Krysztofinska, Arjun Thapaliya, Alessandro Spilotros, Dijana Matak-Vinkovic, Enrico Salvadori, Peristera Roboti, Yvonne Nyathi, Janina H. Muench, Maxie M. Roessler, Dmitri I. Svergun, Stephen High, Rivka L. Isaacson
Format: Article
Language:English
Published: BMC 2018-07-01
Series:BMC Biology
Online Access:http://link.springer.com/article/10.1186/s12915-018-0542-3

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http://link.springer.com/article/10.1186/s12915-018-0542-3

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