Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F18%3A43897644" target="_blank" >RIV/60076658:12310/18:43897644 - isvavai.cz</a>
Alternative codes found
RIV/60077344:_____/18:00499993
Result on the web
<a href="https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1007326" target="_blank" >https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1007326</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.ppat.1007326" target="_blank" >10.1371/journal.ppat.1007326</a>
Alternative languages
Result language
angličtina
Original language name
Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei
Original language description
Fe-S clusters are ubiquitous cofactors of proteins involved in a variety of essential cellular processes. The biogenesis of Fe-S clusters in the cytosol and their insertion into proteins is accomplished through the cytosolic iron-sulphur protein assembly (CIA) machinery. The early- and middle-acting modules of the CIA pathway concerned with the assembly and trafficking of Fe-S clusters have been previously characterised in the parasitic protist Trypanosoma brucei. In this study, we applied proteomic and genetic approaches to gain insights into the network of protein-protein interactions of the late-acting CIA targeting complex in T. brucei. All components of the canonical CIA machinery are present in T. brucei including, as in humans, two distinct CIA2 homologues TbCIA2A and TbCIA2B. These two proteins are found interacting with TbCIA1, yet the interaction is mutually exclusive, as determined by mass spectrometry. Ablation of most of the components of the CIA targeting complex by RNAi led to impaired cell growth in vitro, with the exception of TbCIA2A in procyclic form (PCF) trypanosomes. Depletion of the CIA-targeting complex was accompanied by reduced levels of protein-bound cytosolic iron and decreased activity of an Fe-S dependent enzyme in PCF trypanosomes. We demonstrate that the C-terminal domain of TbMMS19 acts as a docking site for TbCIA2B and TbCIA1, forming a trimeric complex that also interacts with target Fe-S apo-proteins and the middle-acting CIA component TbNAR1.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
PLoS Pathogens
ISSN
1553-7366
e-ISSN
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Volume of the periodical
14
Issue of the periodical within the volume
10
Country of publishing house
US - UNITED STATES
Number of pages
31
Pages from-to
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UT code for WoS article
000448978700021
EID of the result in the Scopus database
2-s2.0-85055901583