Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules
about
The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane.Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complexTim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membraneA genomewide screen for petite-negative yeast strains yields a new subunit of the i-AAA protease complex.Division of mitochondria requires a novel DMN1-interacting protein, Net2pJuxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10.Dual interaction of scaffold protein Tim44 of mitochondrial import motor with channel-forming translocase subunit Tim23Architecture of the TIM23 inner mitochondrial translocon and interactions with the matrix import motorThe Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein importActivation of the pleiotropic drug resistance pathway can promote mitochondrial DNA retention by fusion-defective mitochondria in Saccharomyces cerevisiae.Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiaeProtein import into mitochondria: origins and functions today (review).Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria.Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membraneQuaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits.Tim23p contains separate and distinct signals for targeting to mitochondria and insertion into the inner membrane.Role of the negative charges in the cytosolic domain of TOM22 in the import of precursor proteins into mitochondria.Tim50, a novel component of the TIM23 preprotein translocase of mitochondria.Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplexBacterial tail anchors can target to the mitochondrial outer membrane.Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import.A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import.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.The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.
P2860
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P2860
Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Characterization of the mitoch ...... ot with other Tim23p molecules
@en
Characterization of the mitoch ...... t with other Tim23p molecules.
@nl
type
label
Characterization of the mitoch ...... ot with other Tim23p molecules
@en
Characterization of the mitoch ...... t with other Tim23p molecules.
@nl
prefLabel
Characterization of the mitoch ...... ot with other Tim23p molecules
@en
Characterization of the mitoch ...... t with other Tim23p molecules.
@nl
P2093
P2860
P356
P1476
Characterization of the mitoch ...... ot with other Tim23p molecules
@en
P2093
P2860
P304
P356
10.1128/MCB.18.1.178
P407
P577
1998-01-01T00:00:00Z