scholarly journals Cryptic mitochondrial targeting signals in human ARF: Clues to controlling cancer?

Cell Cycle ◽  
2010 ◽  
Vol 9 (5) ◽  
pp. 861-869
Author(s):  
Beric R. Henderson
2019 ◽  
Author(s):  
Viraj Muthye ◽  
Dennis Lavrov

AbstractDespite a conserved set of core mitochondrial functions, animal mitochondrial proteomes show a large variation in size. In this study, we analyzed the putative mechanisms behind and functional significance of this variation using experimentally-verified mt-proteomes of four bilaterian animals and two non-animal outgroups. We found that, of several factors affecting mitochondrial proteome size, evolution of novel mitochondrial proteins in mammals and loss of ancestral proteins in protostomes were the main contributors. Interestingly, gain and loss of conventional mitochondrial targeting signals was not a significant factor in the proteome size evolution.


2002 ◽  
Vol 277 (32) ◽  
pp. 28757-28764 ◽  
Author(s):  
Roland Schricker ◽  
Michaela Angermayr ◽  
Gertrud Strobel ◽  
Sigrid Klinke ◽  
Dorothee Korber ◽  
...  

2022 ◽  
Vol 12 ◽  
Author(s):  
Marcel G. Genge ◽  
Dejana Mokranjac

The vast majority of mitochondrial proteins are encoded in the nuclear genome and synthesized on cytosolic ribosomes as precursor proteins with specific mitochondrial targeting signals. Mitochondrial targeting signals are very diverse, however, about 70% of mitochondrial proteins carry cleavable, N-terminal extensions called presequences. These amphipathic helices with one positively charged and one hydrophobic surface target proteins to the mitochondrial matrix with the help of the TOM and TIM23 complexes in the outer and inner membranes, respectively. Translocation of proteins across the two mitochondrial membranes does not take place independently of each other. Rather, in the intermembrane space, where the two complexes meet, components of the TOM and TIM23 complexes form an intricate network of protein–protein interactions that mediates initially transfer of presequences and then of the entire precursor proteins from the outer to the inner mitochondrial membrane. In this Mini Review, we summarize our current understanding of how the TOM and TIM23 complexes cooperate with each other and highlight some of the future challenges and unresolved questions in the field.


2005 ◽  
Vol 334 (3) ◽  
pp. 939-946 ◽  
Author(s):  
Sonja C. Stadler ◽  
Roman Polanetz ◽  
Stephan Meier ◽  
Peter U. Mayerhofer ◽  
Johannes M. Herrmann ◽  
...  

2018 ◽  
Author(s):  
Carolina Río Bártulos ◽  
Matthew B. Rogers ◽  
Tom A. Williams ◽  
Eleni Gentekaki ◽  
Henner Brinkmann ◽  
...  

Glycolysis is a major cytosolic catabolic pathway that provides ATP for many organisms1. Mitochondria play an even more important role in the provision of additional cellular ATP for eukaryotes2. Here, we show that in many stramenopiles, the C3 part of glycolysis is localised in mitochondria. We discovered genuine mitochondrial targeting signals on the six last enzymes of glycolysis. These targeting signals are recognised and sufficient to import GFP into mitochondria of a heterologous host. Analysis of eukaryotic genomes identified these targeting signals on many glycolytic C3 enzymes in a large group of eukaryotes found in the SAR supergroup3, in particular the stramenopiles. Stramenopiles, or heterokonts, are a large group of ecologically important eukaryotes that includes multi- and unicellular algae such as kelp and diatoms, but also economically important oomycete pathogens such as Phytophthora infestans. Confocal immunomicroscopy confirmed the mitochondrial location of glycolytic enzymes for the human parasite Blastocystis. Enzyme assays on cellular fractions confirmed the presence of the C3 part of glycolysis in Blastocystis mitochondria. These activities are sensitive to treatment with proteases and Triton X-100 but not proteases alone. Our work clearly shows that core cellular metabolism is more plastic than previously imagined and suggests new strategies to combat stramenopile pathogens such as the causative agent of late potato blight, P. infestans.


2014 ◽  
Vol 31 (9) ◽  
pp. 2503-2515 ◽  
Author(s):  
Karina J. Matissek ◽  
Abood Okal ◽  
Mohanad Mossalam ◽  
Carol S. Lim

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