Journal Article

FZJ-2023-00943

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Preproteins couple the intrinsic dynamics of SecA to its ATPase cycle to translocate via a catch and release mechanism

Krishnamurthy, S. ; Sardis, M.-F. ; Eleftheriadis, N. ; Chatzi, K. E. ; Smit, J. H. ; Karathanou, K. ; Gouridis, G. ; Portaliou, A. G. ; Bondar, A.-N.FZJ* ; Karamanou, S. ; Economou, A. (Corresponding author)

2022
Elsevier [New York, NY]

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Please use a persistent id in citations: http://hdl.handle.net/2128/33767  doi:10.1016/j.celrep.2022.110346

Abstract: Protein machines undergo conformational motions to interact with and manipulate polymeric substrates. The Sec translocase promiscuously recognizes, becomes activated, and secretes >500 non-folded preprotein clients across bacterial cytoplasmic membranes. Here, we reveal that the intrinsic dynamics of the translocase ATPase, SecA, and of preproteins combine to achieve translocation. SecA possesses an intrinsically dynamic preprotein clamp attached to an equally dynamic ATPase motor. Alternating motor conformations are finely controlled by the γ-phosphate of ATP, while ADP causes motor stalling, independently of clamp motions. Functional preproteins physically bridge these independent dynamics. Their signal peptides promote clamp closing; their mature domain overcomes the rate-limiting ADP release. While repeated ATP cycles shift the motor between unique states, multiple conformationally frustrated prongs in the clamp repeatedly “catch and release” trapped preprotein segments until translocation completion. This universal mechanism allows any preprotein to promiscuously recognize the translocase, usurp its intrinsic dynamics, and become secreted.

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Contributing Institute(s):

1. Computational Biomedicine (IAS-5)
2. Computational Biomedicine (INM-9)

Research Program(s):

1. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2022

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Database coverage:
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