(Q44570568)

4 December 2017

title

Structural changes in the mitochondrial Tim23 channel are coupled to the proton-motive force (English)

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4 December 2017

1

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4 December 2017

2

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4 December 2017

Murugappan Sathappa

3

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4 December 2017

Judith S Landin

series ordinal

4

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4 December 2017

Arthur E Johnson

series ordinal

5

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4 December 2017

Nathan N Alder

series ordinal

6

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4 December 2017

language of work or name

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7 July 2013

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Nature Structural & Molecular Biology

4 December 2017

published in

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4 December 2017

volume

20

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4 December 2017

issue

8

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4 December 2017

page(s)

965-972

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https://scigraph.springernature.com/pub.10.1038/nsmb.2613

4 December 2017

exact match

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cites work

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Understanding the molecular mechanism of protein translocation across the mitochondrial inner membrane: still a long way to go.

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A presequence- and voltage-sensitive channel of the mitochondrial preprotein translocase formed by Tim23.

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Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes

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Direct interaction of mitochondrial targeting presequences with purified components of the TIM23 protein complex

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Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex

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Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes

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Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting

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Role of Tim21 in mitochondrial translocation contact sites

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Tim23-Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import

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Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain

21 January 2018

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Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism

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TIM23-mediated insertion of transmembrane α-helices into the mitochondrial inner membrane.

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Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC.

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Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria

21 January 2018

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Tim50 maintains the permeability barrier of the mitochondrial inner membrane

21 January 2018

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Protein unfolding by the mitochondrial membrane potential

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Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits

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Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the deltapsi-dependence of translocation of the matrix-targeting sequence

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During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria

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Polypeptides traverse the mitochondrial envelope in an extended state

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Fluorescence mapping of mitochondrial TIM23 complex reveals a water-facing, substrate-interacting helix surface

31 March 2020

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Tim17p regulates the twin pore structure and voltage gating of the mitochondrial protein import complex TIM23

31 March 2020

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31 March 2020

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31 March 2020

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31 March 2020

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The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation

31 March 2020

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Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondria

31 March 2020

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12 December 2020

The mitochondrial presequence translocase: an essential role of Tim50 in directing preproteins to the import channel

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12 December 2020

Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria

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12 December 2020

Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences

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12 December 2020

Identifiers

DOI

10.1038/NSMB.2613

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Dimensions Publication ID

4 December 2017

1044045553

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