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Thursday, 13 January, 2011

A finishing school for proteins

Deciphering the conformational cycle of the molecular chaperone BiP

 

© Nature Structural & Molecular Biology, doi:10.1038/nsmb.1970, 2011

Proteins form the labour force of the cell. Each protein can perform its particular function only if it folds into a specific shape. Misfolded proteins have a strong tendency to clump, forming insoluble aggregates that are associated with serious disabilities such as Alzheimer’s, Parkinson’s and Huntington’s diseases. Molecular chaperones (so called because they favorably influence the behaviour of their substrates) intervene, often during protein synthesis, to prevent such misfolding. A team led by Professors Don C. Lamb of the Department of Chemistry at LMU Munich and Johannes Buchner of the Technische Universität (TU) München have now taken a closer look at how a major chaperone called BiP performs this role. The researchers specifically asked how BiP’s conformation changes from the moment it binds to a substrate up until the substrate is released and how the co-chaperone ERdJ3 influences its functional cycle. To follow conformational changes, the team made use of a technique known as FRET (Förster Resonance Energy Transfer), which allows one to measure distances (on the order of nanometers) within and between interacting proteins. The results show that two large domains in BiP interact with each other, and that ErdJ3 modulates this interaction in a striking way. (Nature Structural & Molecular Biology online, 9. January 2011)

 

Press information LMU (english)
Presseinformation der LMU (deutsch)
Publication "Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions"