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Rearranging AAA+ architecture to accommodate folded substrates

Nature Structural & Molecular Biology volume 27, pages 225–226 (2020)Cite this article

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Many AAA+ ATPases assemble as hexamers to unfold protein substrates using a hand-over-hand, threading mechanism, but the Bcs1 AAA+ ATPase facilitates mitochondrial membrane translocation of the folded iron–sulfur Rieske protein. Two reports reveal that Bcs1 adopts an unusual heptameric configuration and provide insights into a non-canonical translocation mechanism.

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Fig. 1: Topogenesis of the Rieske iron–sulfur protein, Rip1, by the Bcs1 AAA+ ATPase.
Fig. 2: Structure of the Bcs1 heptamer.

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  1. Department of Biochemistry, School of Medicine, University of Utah, Salt Lake City, UT, USA

    Peter S. Shen

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  1. Peter S. Shen
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Correspondence to Peter S. Shen.

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Shen, P.S. Rearranging AAA+ architecture to accommodate folded substrates. Nat Struct Mol Biol 27, 225–226 (2020). https://doi.org/10.1038/s41594-020-0389-5

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