DOI: 10.1083/jcb.200709087. Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain

Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain

10.1083/jcb.200709087

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

The mitochondrial presequence translocase transports preproteins to either matrix or inner membrane. Two different translocase forms have been identified: the matrix transport form, which binds the heat-shock protein 70 (Hsp70) motor, and the inner membrane–sorting form, which lacks the motor but contains translocase of inner mitochondrial membrane 21 (Tim21). The sorting form interacts with the respiratory chain in a Tim21-dependent manner. It is unknown whether the respiratory chain–bound translocase transports preproteins and how the switch between sorting form and motor form occurs. We report that the respiratory chain–bound translocase contains preproteins in transit and, surprisingly, not only sorted but also matrix-targeted preproteins. Presequence translocase-associated motor (Pam) 16 and 18, two regulatory components of the six-subunit motor, interact with the respiratory chain independently of Tim21. Thus, the respiratory chain–bound presequence translocase is not only active in preprotein sorting to the inner membrane but also in an early stage of matrix translocation. The motor does not assemble en bloc with the translocase but apparently in a step-wise manner with the Pam16/18 module before the Hsp70 core.

Bibliography

Wiedemann, N., van der Laan, M., Hutu, D. P., Rehling, P., & Pfanner, N. (2007). Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain. The Journal of Cell Biology, 179(6), 1115â1122.

Authors 5

Nils Wiedemann (first)
Martin van der Laan (additional)
Dana P. Hutu (additional)
Peter Rehling (additional)
Nikolaus Pfanner (additional)

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Dates

Type	When
Created	17 years, 8 months ago (Dec. 10, 2007, 8:34 p.m.)
Deposited	2 years, 1 month ago (July 29, 2023, 11:17 a.m.)
Indexed	3 months, 3 weeks ago (May 9, 2025, 4:46 a.m.)
Issued	17 years, 8 months ago (Dec. 10, 2007)
Published	17 years, 8 months ago (Dec. 10, 2007)
Published Online	17 years, 8 months ago (Dec. 10, 2007)
Published Print	17 years, 8 months ago (Dec. 17, 2007)

Funders 0

None

BibTeX

@article{Wiedemann_2007, title={Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain}, volume={179}, ISSN={0021-9525}, url={http://dx.doi.org/10.1083/jcb.200709087}, DOI={10.1083/jcb.200709087}, number={6}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Wiedemann, Nils and van der Laan, Martin and Hutu, Dana P. and Rehling, Peter and Pfanner, Nikolaus}, year={2007}, month=dec, pages={1115–1122} }

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  "abstract": "<jats:p>The mitochondrial presequence translocase transports preproteins to either matrix or inner membrane. Two different translocase forms have been identified: the matrix transport form, which binds the heat-shock protein 70 (Hsp70) motor, and the inner membrane\u2013sorting form, which lacks the motor but contains translocase of inner mitochondrial membrane 21 (Tim21). The sorting form interacts with the respiratory chain in a Tim21-dependent manner. It is unknown whether the respiratory chain\u2013bound translocase transports preproteins and how the switch between sorting form and motor form occurs. We report that the respiratory chain\u2013bound translocase contains preproteins in transit and, surprisingly, not only sorted but also matrix-targeted preproteins. Presequence translocase-associated motor (Pam) 16 and 18, two regulatory components of the six-subunit motor, interact with the respiratory chain independently of Tim21. Thus, the respiratory chain\u2013bound presequence translocase is not only active in preprotein sorting to the inner membrane but also in an early stage of matrix translocation. The motor does not assemble en bloc with the translocase but apparently in a step-wise manner with the Pam16/18 module before the Hsp70 core.</jats:p>",
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