Analysis of Mdm38 function in mitochondrial translation

by Jan-Moritz Wuttke
Doctoral thesis
Date of Examination:2015-09-03
Date of issue:2015-11-05
Advisor:Prof. Dr. Peter Rehling
Referee:Prof. Dr. Peter Rehling
Referee:PD Dr. Wilfried Kramer
Persistent Address: http://dx.doi.org/10.53846/goediss-5350

 

 

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Abstract

English

The data presented in this thesis demonstrate that binding of Mdm38 to ribosomes has conserved characteristics in yeast and E. coli. To gain further insights into potential binding partners, an in vivo photo cross-linking assay was established. Here, preliminary mass spectrometry analysis of a specific cross-linked product revealed proteins involved in pre- and post-translational steps. Nevertheless, further studies are required to improve purifications and to enable the analysis of lower molecular weight proteins. Further, it was shown that a fusion of the biotin ligase, BirA, to Mdm38 can be used as a tool to identify proteins in the proximity of Mdm38 in yeast. The comparison of present findings to those from previous studies implies a correlation between transcription and translation involving Mdm38. Finally, this thesis demonstrates a novel overexpression phenotype for Mdm38, which resembles characteristics of the MDM38 deletion mutant. Data presented here argue against an effect attributed to the proteins role in ion-homeostasis, but rather suggest an influence on post-translational processes, causing the respective phenotypes. However, further experiments are required to address possible effects of Mdm38-overexpression on the assembly of respiratory chain complexes.
Keywords: Mitochondria; Mdm38; Yeast; S. cerevisiae
 
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