Distribution and Functional Analysis of Isocitrate Dehydrogenases across Kinetoplastids

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00584660" target="_blank" >RIV/60077344:_____/24:00584660 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61988987:17310/24:A2502O8S RIV/00216208:11310/24:10479660

Výsledek na webu

<a href="https://doi.org/10.1093/gbe/evae042" target="_blank" >https://doi.org/10.1093/gbe/evae042</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/gbe/evae042" target="_blank" >10.1093/gbe/evae042</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Distribution and Functional Analysis of Isocitrate Dehydrogenases across Kinetoplastids

Popis výsledku v původním jazyce

Isocitrate dehydrogenase is an enzyme converting isocitrate to alpha-ketoglutarate in the canonical tricarboxylic acid (TCA) cycle. There are three different types of isocitrate dehydrogenase documented in eukaryotes. Our study points out the complex evolutionary history of isocitrate dehydrogenases across kinetoplastids, where the common ancestor of Trypanosomatidae and Bodonidae was equipped with two isoforms of the isocitrate dehydrogenase enzyme: the NADP(+)-dependent isocitrate dehydrogenase 1 with possibly dual localization in the cytosol and mitochondrion and NADP(+)-dependent mitochondrial isocitrate dehydrogenase 2. In the extant trypanosomatids, isocitrate dehydrogenase 1 is present only in a few species suggesting that it was lost upon separation of Trypanosoma spp. and replaced by the mainly NADP+-dependent cytosolic isocitrate dehydrogenase 3 of bacterial origin in all the derived lineages. In this study, we experimentally demonstrate that the omnipresent isocitrate dehydrogenase 2 has a dual localization in both mitochondrion and cytosol in at least four species that possess only this isoform. The apparent lack of the NAD(+)-dependent isocitrate dehydrogenase activity in trypanosomatid mitochondrion provides further support to the existence of the noncanonical TCA cycle across trypanosomatids and the bidirectional activity of isocitrate dehydrogenase 3 when operating with NADP(+) cofactor instead of NAD(+). This observation can be extended to all 17 species analyzed in this study, except for Leishmania mexicana, which showed only low isocitrate dehydrogenase activity in the cytosol. The variability in isocitrate oxidation capacity among species may reflect the distinct metabolic strategies and needs for reduced cofactors in particular environments.

Název v anglickém jazyce

Distribution and Functional Analysis of Isocitrate Dehydrogenases across Kinetoplastids

Popis výsledku anglicky

Isocitrate dehydrogenase is an enzyme converting isocitrate to alpha-ketoglutarate in the canonical tricarboxylic acid (TCA) cycle. There are three different types of isocitrate dehydrogenase documented in eukaryotes. Our study points out the complex evolutionary history of isocitrate dehydrogenases across kinetoplastids, where the common ancestor of Trypanosomatidae and Bodonidae was equipped with two isoforms of the isocitrate dehydrogenase enzyme: the NADP(+)-dependent isocitrate dehydrogenase 1 with possibly dual localization in the cytosol and mitochondrion and NADP(+)-dependent mitochondrial isocitrate dehydrogenase 2. In the extant trypanosomatids, isocitrate dehydrogenase 1 is present only in a few species suggesting that it was lost upon separation of Trypanosoma spp. and replaced by the mainly NADP+-dependent cytosolic isocitrate dehydrogenase 3 of bacterial origin in all the derived lineages. In this study, we experimentally demonstrate that the omnipresent isocitrate dehydrogenase 2 has a dual localization in both mitochondrion and cytosol in at least four species that possess only this isoform. The apparent lack of the NAD(+)-dependent isocitrate dehydrogenase activity in trypanosomatid mitochondrion provides further support to the existence of the noncanonical TCA cycle across trypanosomatids and the bidirectional activity of isocitrate dehydrogenase 3 when operating with NADP(+) cofactor instead of NAD(+). This observation can be extended to all 17 species analyzed in this study, except for Leishmania mexicana, which showed only low isocitrate dehydrogenase activity in the cytosol. The variability in isocitrate oxidation capacity among species may reflect the distinct metabolic strategies and needs for reduced cofactors in particular environments.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LUASK22033" target="_blank" >LUASK22033: Biochemie trypanosmoatid: pohled ze strany přehlížených druhů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

Genome Biology and Evolution

ISSN

1759-6653

e-ISSN

1759-6653

Svazek periodika

16

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

evae042

Kód UT WoS článku

001186413600001

EID výsledku v databázi Scopus

2-s2.0-85188150345