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The core components of organelle biogenesis and membrane transport in the hydrogenosomes of Trichomonas vaginalis  

Rada, Petr, Dolezal, Pavel, Jedelsky, Petra L., Bursać, Dejan, Perry, Andrew J., Sedinova, Miroslava, Smiskova, Katerina, Novotny, Marian, Beltran, Neritza Campo, Hrdy, Ivan, Lithgow, Trevor and Tachezy, Jan 2011, The core components of organelle biogenesis and membrane transport in the hydrogenosomes of Trichomonas vaginalis  , PLoS one, vol. 6, no. 9, pp. 1-16, doi: 10.1371/journal.pone.0024428.

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Title The core components of organelle biogenesis and membrane transport in the hydrogenosomes of Trichomonas vaginalis  
Formatted title The core components of organelle biogenesis and membrane transport in the hydrogenosomes of Trichomonas vaginalis
Author(s) Rada, Petr
Dolezal, Pavel
Jedelsky, Petra L.
Bursać, Dejan
Perry, Andrew J.
Sedinova, Miroslava
Smiskova, Katerina
Novotny, Marian
Beltran, Neritza Campo
Hrdy, Ivan
Lithgow, Trevor
Tachezy, Jan
Journal name PLoS one
Volume number 6
Issue number 9
Article ID e24428
Start page 1
End page 16
Total pages 16
Publisher Public Library of Science
Place of publication San Francisco, Calif.
Publication date 2011-09-15
ISSN 1932-6203
Keyword(s) Trichomonas vaginalis
core components
organelle biogenesis
membrane transport
hydrogenosomes
Summary Trichomonas vaginalis is a parasitic protist of the Excavata group. It contains an anaerobic form of mitochondria called hydrogenosomes, which produce hydrogen and ATP; the majority of mitochondrial pathways and the organellar genome were lost during the mitochondrion-to-hydrogenosome transition. Consequently, all hydrogenosomal proteins are encoded in the nucleus and imported into the organelles. However, little is known about the membrane machineries required for biogenesis of the organelle and metabolite exchange. Using a combination of mass spectrometry, immunofluorescence microscopy, in vitro import assays and reverse genetics, we characterized the membrane proteins of the hydrogenosome. We identified components of the outer membrane (TOM) and inner membrane (TIM) protein translocases include multiple paralogs of the core Tom40-type porins and Tim17/22/23 channel proteins, respectively, and uniquely modified small Tim chaperones. The inner membrane proteins TvTim17/22/23-1 and Pam18 were shown to possess conserved information for targeting to mitochondrial inner membranes, but too divergent in sequence to support the growth of yeast strains lacking Tim17, Tim22, Tim23 or Pam18. Full complementation was seen only when the J-domain of hydrogenosomal Pam18 was fused with N-terminal region and transmembrane segment of the yeast homolog. Candidates for metabolite exchange across the outer membrane were identified including multiple isoforms of the β-barrel proteins, Hmp35 and Hmp36; inner membrane MCF-type metabolite carriers were limited to five homologs of the ATP/ADP carrier, Hmp31. Lastly, hydrogenosomes possess a pathway for the assembly of C-tail-anchored proteins into their outer membrane with several new tail-anchored proteins being identified. These results show that hydrogenosomes and mitochondria share common core membrane components required for protein import and metabolite exchange; however, they also reveal remarkable differences that reflect the functional adaptation of hydrogenosomes to anaerobic conditions and the peculiar evolutionary history of the Excavata group.
Language eng
DOI 10.1371/journal.pone.0024428
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2011, The Authors
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30064615

Document type: Journal Article
Collections: School of Medicine
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.