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Molecular and Cellular Biology, September 2005, p. 7449-7458, Vol. 25, No. 17
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.17.7449-7458.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Pam17 Is Required for Architecture and Translocation Activity of the Mitochondrial Protein Import Motor

Martin van der Laan,1,{dagger} Agnieszka Chacinska,1,{dagger} Maria Lind,1,{ddagger} Inge Perschil,1 Albert Sickmann,2 Helmut E. Meyer,3 Bernard Guiard,4 Chris Meisinger,1 Nikolaus Pfanner,1* and Peter Rehling1*

Institut für Biochemie und Molekularbiologie, Universität Freiburg, Freiburg,1 Rudolf-Virchow-Center for Experimental Biomedicine, Universität Würzburg, Würzburg,2 Medizinisches Proteom-Center, Ruhr-Universität Bochum, Bochum, Germany,3 Centre de Génétique Moléculaire, Laboratoire propre du CNRS associeté à l'Université Pierre et Marie Curie, Gif-sur-Yvette, France4

Received 29 April 2005/ Returned for modification 7 June 2005/ Accepted 10 June 2005

Import of mitochondrial matrix proteins involves the general translocase of the outer membrane and the presequence translocase of the inner membrane. The presequence translocase-associated motor (PAM) drives the completion of preprotein translocation into the matrix. Five subunits of PAM are known: the preprotein-binding matrix heat shock protein 70 (mtHsp70), the nucleotide exchange factor Mge1, Tim44 that directs mtHsp70 to the inner membrane, and the membrane-bound complex of Pam16-Pam18 that regulates the ATPase activity of mtHsp70. We have identified a sixth motor subunit. Pam17 (encoded by the open reading frame YKR065c) is anchored in the inner membrane and exposed to the matrix. Mitochondria lacking Pam17 are selectively impaired in the import of matrix proteins and the generation of an import-driving activity of PAM. Pam17 is required for formation of a stable complex between the cochaperones Pam16 and Pam18 and promotes the association of Pam16-Pam18 with the presequence translocase. Our findings suggest that Pam17 is required for the correct organization of the Pam16-Pam18 complex and thus contributes to regulation of mtHsp70 activity at the inner membrane translocation site.

* Corresponding author. Mailing address: Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Straße 7, D-79104 Freiburg, Germany. Phone: 49-761-203-5224. Fax: 49-761-203-5261. E-mail for Nikolaus Pfanner: Nikolaus.Pfanner{at}biochemie.uni-freiburg.de. E-mail for Peter Rehling: Peter.Rehling{at}biochemie.uni-freiburg.de.

{dagger} M.V.D.L. and A.C. contributed equally to this work.

{ddagger} Present address: Department of Comparative Physiology, Evolutionary Biology Centre, Uppsala University, SE-75236 Uppsala, Sweden.

Molecular and Cellular Biology, September 2005, p. 7449-7458, Vol. 25, No. 17
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.17.7449-7458.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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