A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein.
about
The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.The plastid genome of Cryptomonas phi encodes an hsp70-like protein, a histone-like protein, and an acyl carrier proteinThe proteome of Saccharomyces cerevisiae mitochondria.Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast.A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocationDynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membraneMolecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria.Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.Loss of mitochondrial hsp60 function: nonequivalent effects on matrix-targeted and intermembrane-targeted proteins.Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondriaMPI1, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondriaPresequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix.A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viabilityMitochondrial biogenesis during germination in maize embryosThe mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.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.Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunitsRole of ATP in the intramitochondrial sorting of cytochrome c1 and the adenine nucleotide translocator.Translocation can drive the unfolding of a preprotein domain.Strong precursor-pore interactions constrain models for mitochondrial protein importSignaling the mitochondrial unfolded protein response.Heat shock proteins: molecular chaperones of protein biogenesis.Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix.PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein.Barth syndrome mutations that cause tafazzin complex lability.In vivo and in vitro interaction of DnaK and a chloroplast transit peptide.Altered zinc transport disrupts mitochondrial protein processing/import in fragile X-associated tremor/ataxia syndrome.Outer membrane translocation arrest of the TcpA pilin subunit in rfb mutants of Vibrio cholerae O1 strain 569B.Sequential action of mitochondrial chaperones in protein import into the matrixBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Intramitochondrial sorting of the precursor to yeast cytochrome c oxidase subunit Va.A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins.Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysisTargeting proteins to mitochondria: a current overview.Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptidesIndividual subunits of bacterial luciferase are molten globules and interact with molecular chaperones.
P2860
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P2860
A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein.
description
1990 nî lūn-bûn
@nan
1990 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
A precursor protein partly tra ...... mitochondrial stress protein.
@ast
A precursor protein partly tra ...... mitochondrial stress protein.
@en
type
label
A precursor protein partly tra ...... mitochondrial stress protein.
@ast
A precursor protein partly tra ...... mitochondrial stress protein.
@en
prefLabel
A precursor protein partly tra ...... mitochondrial stress protein.
@ast
A precursor protein partly tra ...... mitochondrial stress protein.
@en
P2093
P2860
P1433
P1476
A precursor protein partly tra ...... d mitochondrial stress protein
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1990.TB07880.X
P407
P577
1990-12-01T00:00:00Z