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Medizin - Open Access LMU - Teil 11/22 Podcast
Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria

Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria

Medizin - Open Access LMU - Teil 11/22 vor 31 Jahren

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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 with 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.