Trypanosoma brucei Mitochondrial Respiratome: Composition and Organization in Procyclic Form

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F11%3A00367704" target="_blank" >RIV/60077344:_____/11:00367704 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1074/mcp.M110.006908" target="_blank" >http://dx.doi.org/10.1074/mcp.M110.006908</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/mcp.M110.006908" target="_blank" >10.1074/mcp.M110.006908</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Trypanosoma brucei Mitochondrial Respiratome: Composition and Organization in Procyclic Form

Popis výsledku v původním jazyce

The mitochondrial respiratory chain is comprised of four different protein complexes (I-IV), which are responsible for electron transport and generation of proton gradient in the mitochondrial intermembrane space. In this study, the respiratory complexesI, II, and III were affinity purified from Trypanosoma brucei procyclic form cells and their composition was determined by mass spectrometry. The results showed that the respiratome of Trypanosoma is divergent because many of its proteins are unique tothis group of organisms. Proteomics data from analyses of complexes purified using numerous tagged component proteins in each of the five complexes were used to generate the first predicted protein-protein interaction network of the Trypanosoma brucei respiratory chain. These results provide the first comprehensive insight into the unique composition of the respiratory complexes in Trypanosoma brucei, an early diverged eukaryotic pathogen.

Název v anglickém jazyce

Trypanosoma brucei Mitochondrial Respiratome: Composition and Organization in Procyclic Form

Popis výsledku anglicky

The mitochondrial respiratory chain is comprised of four different protein complexes (I-IV), which are responsible for electron transport and generation of proton gradient in the mitochondrial intermembrane space. In this study, the respiratory complexesI, II, and III were affinity purified from Trypanosoma brucei procyclic form cells and their composition was determined by mass spectrometry. The results showed that the respiratome of Trypanosoma is divergent because many of its proteins are unique tothis group of organisms. Proteomics data from analyses of complexes purified using numerous tagged component proteins in each of the five complexes were used to generate the first predicted protein-protein interaction network of the Trypanosoma brucei respiratory chain. These results provide the first comprehensive insight into the unique composition of the respiratory complexes in Trypanosoma brucei, an early diverged eukaryotic pathogen.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

<a href="/cs/project/GP204%2F09%2FP563" target="_blank" >GP204/09/P563: Funkční analýza dvou nových podjednotek komplexu F0F1-ATP syntázy u Trypanosoma brucei</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Molecular and Cellular Proteomics

ISSN

1535-9476

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

14

Strana od-do

1-14

Kód UT WoS článku

000294729200007

EID výsledku v databázi Scopus

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