publication . Article . Other literature type . 2005

Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane

D'Silva P. R.; Schilke B.; Walter W.; Craig E. A.;
Open Access
  • Published: 16 Aug 2005 Journal: Proceedings of the National Academy of Sciences, volume 102, pages 12,419-12,424 (issn: 0027-8424, eissn: 1091-6490, Copyright policy)
  • Publisher: Proceedings of the National Academy of Sciences
Abstract
Translocation of proteins across the mitochondrial inner membrane is an essential process requiring an import motor having mitochondrial Hsp70 (mtHsp70) at its core. The J protein partner of mtHsp70, Pam18, is an integral part of this motor, serving to stimulate the ATPase activity of mtHsp70. Pam16, an essential protein having an inactive J domain that is unable to stimulate mtHsp70's ATPase activity, forms a heterodimer with Pam18, but its function is unknown. We set out to test the importance of three properties of Pam16: (i) a stable interaction between Pam16 and Pam18, (ii) the inability of Pam16's degenerate J domain to stimulate Ssc1's ATPase domain, and ...
Subjects
free text keywords: Multidisciplinary, ATPase, biology.protein, biology, Inner mitochondrial membrane, Saccharomyces cerevisiae, biology.organism_classification, Mitochondrial membrane transport protein, Cell biology, Chaperone (protein), Cell growth, Membrane transport protein, Mitochondrion, Biological Sciences
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