Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
about
Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membraneThe Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complexA new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implicationsTim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondriaThe J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase.The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane.The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein importBiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins.Pam17 is required for architecture and translocation activity of the mitochondrial protein import motorDifferential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.Modular structure of the TIM23 preprotein translocase of mitochondria.Tim9, a new component of the TIM22.54 translocase in mitochondriaMitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70The DNA helicase, Hmi1p, is transported into mitochondria by a C-terminal cleavable targeting signal.Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathwayCarrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5.Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tetheringThe mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.Posttranslational protein translocation across the membrane of the endoplasmic reticulum.Mitochondrial disorders. A diagnostic challenge in clinical chemistry.Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone.Sequential action of two hsp70 complexes during protein import into mitochondriaActive unfolding of precursor proteins during mitochondrial protein import.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.Protein translocation pathways of the mitochondrion.Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae.Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44.The protein import machinery of the mitochondrial membranes.Strong precursor-pore interactions constrain models for mitochondrial protein importDomain structure and lipid interaction of recombinant yeast Tim44Hsp60-independent protein folding in the matrix of yeast mitochondria.Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linkingTim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC.The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysisTwo intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria.
P2860
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P2860
Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
description
1994 nî lūn-bûn
@nan
1994 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Dynamic interaction between Is ...... t mitochondrial inner membrane
@ast
Dynamic interaction between Is ...... t mitochondrial inner membrane
@en
Dynamic interaction between Is ...... mitochondrial inner membrane.
@nl
type
label
Dynamic interaction between Is ...... t mitochondrial inner membrane
@ast
Dynamic interaction between Is ...... t mitochondrial inner membrane
@en
Dynamic interaction between Is ...... mitochondrial inner membrane.
@nl
prefLabel
Dynamic interaction between Is ...... t mitochondrial inner membrane
@ast
Dynamic interaction between Is ...... t mitochondrial inner membrane
@en
Dynamic interaction between Is ...... mitochondrial inner membrane.
@nl
P2093
P2860
P356
P1476
Dynamic interaction between Is ...... t mitochondrial inner membrane
@en
P2093
L Bolliger
N G Kronidou
W Oppliger
P2860
P304
P356
10.1073/PNAS.91.26.12818
P407
P577
1994-12-20T00:00:00Z