Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion.
Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion.
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DOI:
10.1083/jcb.200706195
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发表时间:
2007-09-24
期刊:
影响因子:
--
通讯作者:
Koehler CM
中科院分区:
文献类型:
--
作者:
Hwang DK;Claypool SM;Leuenberger D;Tienson HL;Koehler CM
Tim54p, a component of the inner membrane TIM22 complex, does not directly mediate the import of inner membrane substrates but is required for assembly/stability of the 300-kD TIM22 complex. In addition, Δtim54 yeast exhibit a petite-negative phenotype (also observed in yeast harboring mutations in the F1Fo ATPase, the ADP/ATP carrier, mitochondrial morphology components, or the i–AAA protease, Yme1p). Interestingly, other import mutants in our strain background are not petite-negative. We report that Tim54p is not involved in maintenance of mitochondrial DNA or mitochondrial morphology. Rather, Tim54p mediates assembly of an active Yme1p complex, after Yme1p is imported via the TIM23 pathway. Defective Yme1p assembly is likely the major contributing factor for the petite-negativity in strains lacking functional Tim54p. Thus, Tim54p has two independent functions: scaffolding/stability for the TIM22 membrane complex and assembly of Yme1p into a proteolytically active complex. As such, Tim54p links protein import, assembly, and turnover pathways in the mitochondrion.
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DOI:
10.1083/jcb.139.7.1663
发表时间:
1997-12-29
期刊:
The Journal of cell biology
影响因子:
--
作者:
Kerscher O;Holder J;Srinivasan M;Leung RS;Jensen RE
通讯作者:
Jensen RE
DOI:
10.1083/jcb.93.1.97
发表时间:
1982-04
期刊:
The Journal of cell biology
影响因子:
--
作者:
Fujiki Y;Hubbard AL;Fowler S;Lazarow PB
通讯作者:
Lazarow PB
影响因子:
3.3
作者:
Dunn, CD;Lee, MS;Jensen, RE
通讯作者:
Jensen, RE
影响因子:
11.4
作者:
HINES, V;BRANDT, A;SCHATZ, G
通讯作者:
SCHATZ, G
影响因子:
3
作者:
Francis, Brian R.;White, Karen H.;Thorsness, Peter E.
通讯作者:
Thorsness, Peter E.