Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane (Q33207985)

23 July 2017

Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane (English)

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23 July 2017

Patrick D'Silva

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23 July 2017

Qinglian Liu

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2

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23 July 2017

William Walter

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3

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23 July 2017

Elizabeth A Craig

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4

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23 July 2017

17 October 2004

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Nature Structural & Molecular Biology

23 July 2017

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23 July 2017

11

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23 July 2017

11

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23 July 2017

1084-1091

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https://scigraph.springernature.com/pub.10.1038/nsmb846

23 July 2017

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cites work

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Opening the door to mitochondrial protein import

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

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

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Protein unfolding by the mitochondrial membrane potential

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

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A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein.

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

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Protein translocation: how Hsp70 pulls it off.

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Mitochondrial Hsp70/MIM44 complex facilitates protein import

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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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Regulated cycling of mitochondrial Hsp70 at the protein import channel

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

31 March 2020

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Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria

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A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria

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J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix

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Pam16 has an essential role in the mitochondrial protein import motor

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Multistep mechanism of substrate binding determines chaperone activity of Hsp70

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

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

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

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A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers

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Structural analysis of substrate binding by the molecular chaperone DnaK

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

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

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

31 March 2020

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The putative helical lid of the Hsp70 peptide-binding domain is required for efficient preprotein translocation into mitochondria

31 March 2020

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Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins.

31 March 2020

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The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains

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Peptide-induced conformational changes in the molecular chaperone DnaK

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Detection of a concerted conformational change in the ATPase domain of DnaK triggered by peptide binding

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Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae

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Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels

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Sequential action of two hsp70 complexes during protein import into mitochondria

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Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart

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Identifiers

DOI

10.1038/NSMB846

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Dimensions Publication ID

23 July 2017

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