Transmembrane Coordination of Preprotein Recognition and Motor Coupling by the Mitochondrial Presequence Receptor Tim50.

Cell Reports
Anne Caumont-SarcosRaffaele Ieva

Abstract

Mitochondrial preproteins contain amino-terminal presequences directing them to the presequence translocase of the mitochondrial inner membrane (TIM23 complex). Depending on additional downstream import signals, TIM23 either inserts preproteins into the inner membrane or translocates them into the matrix. Matrix import requires the coupling of the presequence translocase-associated motor (PAM) to TIM23. The molecular mechanisms coordinating preprotein recognition by TIM23 in the intermembrane space (IMS) with PAM activation in the matrix are unknown. Here we show that subsequent to presequence recognition in the IMS, the Tim50 matrix domain facilitates the recruitment of the coupling factor Pam17. Next, the IMS domain of Tim50 promotes PAM recruitment to TIM23. Finally, the Tim50 transmembrane segment stimulates the matrix-directed import-driving force exerted by PAM. We propose that recognition of preprotein segments in the IMS and transfer of signal information across the inner membrane by Tim50 determine import motor activation.

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Citations

Aug 23, 2020·The Journal of Biological Chemistry·Eva ZöllerJohannes M Herrmann
Apr 20, 2021·Biology of the Cell·Sebabrata Maity, Oishee Chakrabarti
Aug 8, 2021·International Journal of Molecular Sciences·Minu ChaudhuriFidel Soto Gonzalez
Aug 27, 2021·The Biochemical Journal·Fabian den BraveThomas Becker
Oct 1, 2021·Nature Communications·Ridhima GomkalePeter Rehling

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