Protein Quality Control in the Intermembrane Space of Mitochondria

Böttinger, Lena; Becker, Thomas

doi:10.1016/j.jmb.2012.10.013

Cited by 4 publications

(1 citation statement)

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“…2003 ). Despite the presence of dedicated and efficient import machineries, a number of protein quality control pathways exist that remove misfolded and superfluous proteins to prevent faulty complex assembly ( Böttinger and Becker 2012 ; Tatsuta 2009 ). An inefficient complex assembly may lead to ROS production and have deleterious effects on mitochondrial integrity, which in turn can cause various muscular and neurodegenerative disorders in humans ( Nunnari and Suomalainen 2012 ).…”

Section: Introductionmentioning

confidence: 99%

Yme2, a putative RNA recognition motif and AAA+ domain containing protein, genetically interacts with the mitochondrial protein export machinery

Sharma

Osman

2022

Biological Chemistry

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The mitochondrial respiratory chain is composed of nuclear as well as mitochondrial-encoded subunits. A variety of factors mediate co-translational integration of mtDNA-encoded proteins into the inner membrane. In Saccharomyces cerevisiae, Mdm38 and Mba1 are ribosome acceptors that recruit the mitochondrial ribosome to the inner membrane, where the insertase Oxa1, facilitates membrane integration of client proteins. The protein Yme2 has previously been shown to be localized in the inner mitochondrial membrane and has been implicated in mitochondrial protein biogenesis, but its mode of action remains unclear. Here, we show that multiple copies of Yme2 assemble into a high molecular weight complex. Using a combination of bioinformatics and mutational analyses, we find that Yme2 possesses an RNA recognition motif (RRM), which faces the mitochondrial matrix and a AAA+ domain that is located in the intermembrane space. We further show that YME2 genetically interacts with MDM38, MBA1 and OXA1, which links the function of Yme2 to the mitochondrial protein biogenesis machinery.

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Section: Introductionmentioning

confidence: 99%