期刊
NATURE COMMUNICATIONS
卷 9, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-03946-x
关键词
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资金
- Deutsche Forschungsgemeinschaft [SFB 1035 A3/B12]
- Center for Integrated Protein Science Munich (CIPSM)
- Fonds der Chemischen Industrie
- Integrative Metabolism Research Center Graz
- BioTechMed/Graz
- Omics Center Graz
- President's International Fellowship Initiative of CAS [2015VBB045]
- National Natural Science Foundation of China [31450110423]
- Austrian Science Fund [FWF: P28854, W1226-B18]
- Gauss Centre for Supercomputing/Leibniz Supercomputing Centre [pr84pa, pr53po]
- Austrian infrastructure program
- Austrian Science Fund (FWF) [P28854] Funding Source: Austrian Science Fund (FWF)
Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established that conformational switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for switch points in the large middle-domain (Hsp90-M) is scarce. Here we report on a tryptophan residue in Hsp90-M as a new type of switch point. Our study shows that this conserved tryptophan senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-p interaction with a neighboring lysine. Mutations at this position hamper the communication between domains and the ability of a client protein to affect the Hsp90 cycle. The residue thus allows Hsp90 to transmit information on the binding of a client from Hsp90-M to Hsp90-N which is important for progression of the conformational cycle and the efficient processing of client proteins.
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