Molecular Chaperones Cooperate With Pim1 Protease in the Degradation of Misfolded Proteins in Mitochondria
(1994) The EMBO journal — Vol. 13, n° 21, p. 5135-5145 (1994)
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- Abstract
- ATP dependent proteolytic degradation of misfolded proteins in the mitochondrial matrix is mediated by the PIM1 protease and depends on the molecular chaperone proteins mt-hsp70 and Mdj1p. Chaperone function is essential to maintain misfolded proteins in a soluble state, a prerequisite for their degradation by PIM1 protease. In the absence of functional mt-hsp70 or Mdj1p misfolded proteins either remain associated with mt-hsp70 or form aggregates and thereby are no longer substrates for PIM1 protease. Mdj1p is shown to regulate the ATP dependent association of an unfolded polypeptide chain,vith mt-hsp70 affecting binding to as well as release from mt-hsp70. These findings establish a central role of molecular chaperone proteins in the degradation of misfolded proteins by PIM1 protease and thereby demonstrate a functional interrelation between components of the folding machinery and the proteolytic system within mitochondria.
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Citations
Wagner, I., Arlt, H., Vandyck, L., Langer, T., & Neupert, W. (1994). Molecular Chaperones Cooperate With Pim1 Protease in the Degradation of Misfolded Proteins in Mitochondria. The EMBO journal, 13(21), 5135-5145. https://hdl.handle.net/2078.5/145597 (Original work published 1994)