The protein import motor of mitochondria (Q34142481)

31 July 2017

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title

The protein import motor of mitochondria (English)

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31 July 2017

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Walter Neupert

1

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31 July 2017

Michael Brunner

series ordinal

2

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31 July 2017

publication date

1 August 2002

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Nature Reviews Molecular Cell Biology

31 July 2017

published in

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31 July 2017

volume

3

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issue

8

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31 July 2017

page(s)

555-565

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Escherichia coli preprotein translocase

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cites work

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Common principles of protein translocation across membranes

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Protein import into mitochondria

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Protein Translocation: Tunnel Vision

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Protein import into chloroplasts

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The ER translocon and retrotranslocation: is the shift into reverse manual or automatic?

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The protein import machinery of the mitochondrial membranes

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The structural basis of protein targeting and translocation in bacteria.

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Protein translocation machineries of peroxisomes

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Multiple pathways used for the targeting of thylakoid proteins in chloroplasts.

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Mitochondrial preprotein translocase

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Posttranslational protein translocation across the membrane of the endoplasmic reticulum.

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Protein translocation into mitochondria: the role of TIM complexes

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Protein import into mitochondria

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Versatility of the mitochondrial protein import machinery

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The MIM complex mediates preprotein translocationacross the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system

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The TIM17.23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix

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Modular structure of the TIM23 preprotein translocase of mitochondria

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Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22.

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Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5.

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The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane

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Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane

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Import of mitochondrial carriers mediated by essential proteins of the intermembrane space

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Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane

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The role of the TIM8-13 complex in the import of Tim23 into mitochondria

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Tim22, the essential core of the mitochondrial protein insertion complex, forms a voltage-activated and signal-gated channel

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Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria

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Mitochondrial protein import: reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding

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Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment].

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Recognition of preproteins by the isolated TOM complex of mitochondria

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Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria

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Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex

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Probing the environment along the protein import pathways in yeast mitochondria by site-specific photocrosslinking

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Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane

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C- to N-terminal translocation of preproteins into mitochondria

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Tim23 links the inner and outer mitochondrial membranes.

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

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Polypeptides traverse the mitochondrial envelope in an extended state

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The preprotein translocation channel of the outer membrane of mitochondria

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The Structure of Precursor Proteins during Import into Mitochondria

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The dimensions of the protein import channels in the outer and inner mitochondrial membranes

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The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria

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What fuels polypeptide translocation? An energetical view on mitochondrial protein sorting

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Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins

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Protein unfolding by the mitochondrial membrane potential

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Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane

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Mitochondrial Hsp70/MIM44 complex facilitates protein import

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SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein

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Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins

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Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44

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Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane

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Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins

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Specificity of DnaK-peptide binding

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The Hsp70 and Hsp60 Chaperone Machines

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Interaction of Hsp70 chaperones with substrates

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Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

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Molecular basis for interactions of the DnaK chaperone with substrates.

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Multistep mechanism of substrate binding determines chaperone activity of Hsp70

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A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation

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Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins

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The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria

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Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70.

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A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability

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YGE1 is a yeast homologue of Escherichia coli grpE and is required for maintenance of mitochondrial functions

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Yge1p, a eukaryotic Grp-E homolog, is localized in the mitochondrial matrix and interacts with mitochondrial Hsp70

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How do polypeptides cross the mitochondrial membranes?

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What drives the translocation of proteins?

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Mechanisms of translocation of proteins across membranes

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Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.

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Can Hsp70 proteins act as force-generating motors?

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Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44.

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The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation

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Strong precursor-pore interactions constrain models for mitochondrial protein import

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Protein sorting. Pulling in the proteins

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Protein translocation: is Hsp70 pulling my chain?

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Hsp70 proteins in protein translocation

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Chaperone-assisted protein folding.

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Molecular chaperones in cellular protein folding

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Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role

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The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.

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How molecular motors work

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The myosin swinging cross-bridge model.

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Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria.

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Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites

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Unfolding of preproteins upon import into mitochondria

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Sorting of D-lactate dehydrogenase to the inner membrane of mitochondria. Analysis of topogenic signal and energetic requirements

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Mitochondrial import of subunit Va of cytochrome c oxidase characterized with yeast mutants

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The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria

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The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

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Fluorescence quenching: A tool for single-molecule protein-folding study

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Mitochondria Unfold Precursor Proteins by Unraveling Them From Their N-termini

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The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation

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A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins

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Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.

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Protein unfolding by mitochondria. The Hsp70 import motor

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Active unfolding of precursor proteins during mitochondrial protein import

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Mechanical and chemical unfolding of a single protein: a comparison

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Mechanical unfolding intermediates in titin modules.

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Atomic force microscopy reveals the mechanical design of a modular protein.

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Protein folding: pulling back the frontiers.

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What is the driving force for protein import into mitochondria?

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J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences

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BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane

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Identifiers

DOI

10.1038/NRM878

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Dimensions Publication ID

31 July 2017

1050120162

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