Stage-specific requirement for Isa1 and Isa2 proteins in the mitochondrion of Trypanosoma brucei and heterologous rescue by human and Blastocystis orthologues

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F11%3A00365995" target="_blank" >RIV/60077344:_____/11:00365995 - isvavai.cz</a>

Alternative codes found

RIV/60076658:12310/11:43872220

Result on the web

<a href="http://dx.doi.org/10.1111/j.1365-2958.2011.07769.x" target="_blank" >http://dx.doi.org/10.1111/j.1365-2958.2011.07769.x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/j.1365-2958.2011.07769.x" target="_blank" >10.1111/j.1365-2958.2011.07769.x</a>

Result language

angličtina

Original language name

Stage-specific requirement for Isa1 and Isa2 proteins in the mitochondrion of Trypanosoma brucei and heterologous rescue by human and Blastocystis orthologues

Original language description

IscA/Isa proteins function as alternative scaffolds for the assembly of Fe-S clusters and/or provide iron for their assembly in prokaryotes and eukaryotes. We have studied their function in Trypanosoma brucei, where the requirement for both of them to sustain cell growth depends on the life cycle stage. Reactive oxygen species but not iron accumulate in the procyclic mitochondrion upon ablation of the TbIsa proteins, but their depletion does not influence the assembly of Fe-S clusters in cytosolic proteins. In the bloodstream form, which has a downregulated mitochondrion, the TbIsa proteins are non-essential. The Isa2 orthologue of the anaerobic protist Blastocystis partially rescued the growth and enzymatic activities of TbIsa1/2 knock-down. Rescues with human Isa orthologues partially recovered the activities of aconitase and fumarase. These results show that the Isa1 and Isa2 proteins of diverse eukaryotes have overlapping functions.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2011

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecular Microbiology

ISSN

0950-382X

e-ISSN

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Volume of the periodical

81

Issue of the periodical within the volume

6

Country of publishing house

GB - UNITED KINGDOM

Number of pages

16

Pages from-to

1403-1418

UT code for WoS article

000295087000001

EID of the result in the Scopus database

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