St Andrews Research Repository

St Andrews University Home
View Item 
  •   St Andrews Research Repository
  • University of St Andrews Research
  • University of St Andrews Research
  • University of St Andrews Research
  • View Item
  •   St Andrews Research Repository
  • University of St Andrews Research
  • University of St Andrews Research
  • University of St Andrews Research
  • View Item
  •   St Andrews Research Repository
  • University of St Andrews Research
  • University of St Andrews Research
  • University of St Andrews Research
  • View Item
  • Login
JavaScript is disabled for your browser. Some features of this site may not work without it.

Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei

Thumbnail
View/Open
Tonini_2018_PLoSPathogens_Late_steps_CC.pdf (3.670Mb)
Date
22/10/2018
Author
Tonini, Maiko Luis
Peña-Diaz, Priscila
Haindrich, Alexander C.
Basu, Somsuvro
Kriegová, Eva
Pierik, Antonio J.
Lill, Roland
MacNeill, Stuart A.
Smith, Terry K.
Lukeš, Julius
Keywords
QH301 Biology
DAS
BDC
R2C
Metadata
Show full item record
Altmetrics Handle Statistics
Altmetrics DOI Statistics
Abstract
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.
Citation
Tonini , M L , Peña-Diaz , P , Haindrich , A C , Basu , S , Kriegová , E , Pierik , A J , Lill , R , MacNeill , S A , Smith , T K & Lukeš , J 2018 , ' Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei ' , PLoS Pathogens , vol. 14 , no. 10 , e1007326 . https://doi.org/10.1371/journal.ppat.1007326
Publication
PLoS Pathogens
Status
Peer reviewed
DOI
https://doi.org/10.1371/journal.ppat.1007326
ISSN
1553-7366
Type
Journal article
Rights
Copyright: © 2018 Tonini et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description
Support from the Czech Grant Agency (16-18699S to JL) and partial funding by CAPES/Science without Borders (BEX1333/13-5 to MLT) is kindly acknowledged. We are grateful to the University of St. Andrews mass spectrometry facility for collecting and processing MS data and to other members of the TKS and SM groups for their assistance with this project. Work of RL and AJP was supported by the Deutsche Forschungsgemeinschaft (Koselleck grant (to RL) and SPP 1927) and a Coordenação de aperfeiçoamento de pessoal de nivel superior (CAPES - 1333/2013-05) for the financial support to this project. We acknowledge networking support from the COST Action FeSBioNet (Contract CA15133). ERD Funds, The Czech Ministry of Education, project OPVVV 16_019/0000759 to JL.
Collections
  • University of St Andrews Research
URI
http://hdl.handle.net/10023/16382

Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.

Advanced Search

Browse

All of RepositoryCommunities & CollectionsBy Issue DateNamesTitlesSubjectsClassificationTypeFunderThis CollectionBy Issue DateNamesTitlesSubjectsClassificationTypeFunder

My Account

Login

Open Access

To find out how you can benefit from open access to research, see our library web pages and Open Access blog. For open access help contact: openaccess@st-andrews.ac.uk.

Accessibility

Read our Accessibility statement.

How to submit research papers

The full text of research papers can be submitted to the repository via Pure, the University's research information system. For help see our guide: How to deposit in Pure.

Electronic thesis deposit

Help with deposit.

Repository help

For repository help contact: Digital-Repository@st-andrews.ac.uk.

Give Feedback

Cookie policy

This site may use cookies. Please see Terms and Conditions.

Usage statistics

COUNTER-compliant statistics on downloads from the repository are available from the IRUS-UK Service. Contact us for information.

© University of St Andrews Library

University of St Andrews is a charity registered in Scotland, No SC013532.

  • Facebook
  • Twitter