Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.

Abstract:

:The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial "transfer-chaperone" system is able to guide α-helical and β-barrel membrane proteins in a "nascent chain-like" conformation through a ribosome-free compartment.

journal_name

Cell

journal_title

Cell

authors

Weinhäupl K,Lindau C,Hessel A,Wang Y,Schütze C,Jores T,Melchionda L,Schönfisch B,Kalbacher H,Bersch B,Rapaport D,Brennich M,Lindorff-Larsen K,Wiedemann N,Schanda P

doi

10.1016/j.cell.2018.10.039

subject

Has Abstract

pub_date

2018-11-15 00:00:00

pages

1365-1379.e25

issue

5

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(18)31395-3

journal_volume

175

pub_type

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