The Ancestral Shape of the Access Proton Path of Mitochondrial ATP Synthases Revealed by a Split Subunit-a

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F23%3A00574448" target="_blank" >RIV/60077344:_____/23:00574448 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/23:43907130

Výsledek na webu

<a href="https://academic.oup.com/mbe/article/40/6/msad146/7203835?login=true" target="_blank" >https://academic.oup.com/mbe/article/40/6/msad146/7203835?login=true</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/molbev/msad146" target="_blank" >10.1093/molbev/msad146</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The Ancestral Shape of the Access Proton Path of Mitochondrial ATP Synthases Revealed by a Split Subunit-a

Popis výsledku v původním jazyce

The passage of protons across membranes through F1Fo-ATP synthases spins their rotors and drives the synthesis of ATP. While the principle of torque generation by proton transfer is known, the mechanisms and routes of proton access and release and their evolution are not fully understood. Here, we show that the entry site and path of protons in the lumenal half channel of mitochondrial ATP synthases are largely defined by a short N-terminal & alpha,-helix of subunit-a. In Trypanosoma brucei and other Euglenozoa, the & alpha,-helix is part of another polypeptide chain that is a product of subunit-a gene fragmentation. This & alpha,-helix and other elements forming the proton pathway are widely conserved across eukaryotes and in Alphaproteobacteria, the closest extant relatives of mitochondria, but not in other bacteria. The & alpha,-helix blocks one of two proton routes found in Escherichia coli, resulting in a single proton entry site in mitochondrial and alphaproteobacterial ATP synthases. Thus, the shape of the access half channel predates eukaryotes and originated in the lineage from which mitochondria evolved by endosymbiosis.

Název v anglickém jazyce

The Ancestral Shape of the Access Proton Path of Mitochondrial ATP Synthases Revealed by a Split Subunit-a

Popis výsledku anglicky

The passage of protons across membranes through F1Fo-ATP synthases spins their rotors and drives the synthesis of ATP. While the principle of torque generation by proton transfer is known, the mechanisms and routes of proton access and release and their evolution are not fully understood. Here, we show that the entry site and path of protons in the lumenal half channel of mitochondrial ATP synthases are largely defined by a short N-terminal & alpha,-helix of subunit-a. In Trypanosoma brucei and other Euglenozoa, the & alpha,-helix is part of another polypeptide chain that is a product of subunit-a gene fragmentation. This & alpha,-helix and other elements forming the proton pathway are widely conserved across eukaryotes and in Alphaproteobacteria, the closest extant relatives of mitochondria, but not in other bacteria. The & alpha,-helix blocks one of two proton routes found in Escherichia coli, resulting in a single proton entry site in mitochondrial and alphaproteobacterial ATP synthases. Thus, the shape of the access half channel predates eukaryotes and originated in the lineage from which mitochondria evolved by endosymbiosis.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

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

Název periodika

Molecular Biology and Evolution

ISSN

0737-4038

e-ISSN

1537-1719

Svazek periodika

40

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

msad146

Kód UT WoS článku

001021595400005

EID výsledku v databázi Scopus

2-s2.0-85164067501