The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria

The oxidative phosphorylation (OXPHOS) system of mitochondria supports all the vitally important energyconsuming processes in eukaryotic cells, providing them with energy in the form of ATP. OXPHOS enzymes (complexes I–V) are located in the inner mitochondrial membrane, mainly in the cristae subcomp...

Full description

Saved in:
Bibliographic Details
Main Author: I. V. Ukolova
Format: Article
Language:English
Published: Siberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and Breeders 2021-12-01
Series:Вавиловский журнал генетики и селекции
Subjects:
Online Access:https://vavilov.elpub.ru/jour/article/view/3182
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1832575074100576256
author I. V. Ukolova
author_facet I. V. Ukolova
author_sort I. V. Ukolova
collection DOAJ
description The oxidative phosphorylation (OXPHOS) system of mitochondria supports all the vitally important energyconsuming processes in eukaryotic cells, providing them with energy in the form of ATP. OXPHOS enzymes (complexes I–V) are located in the inner mitochondrial membrane, mainly in the cristae subcompartment. At present, there is a large body of data evidencing that the respiratory complexes I, III2 and IV under in vivo conditions can physically interact with each other in diverse stoichiometry, thereby forming supercomplexes. Despite active accumulation of knowledge about the structure of the main supercomplexes of the OXPHOS system, its physical and functional organization in vivo remains unclear. Contemporary models of the OXPHOS system’s organization in the inner membrane of mitochondria are contradictory and presume the existence of either highly organized respiratory strings, or, by contrast, a set of randomly dispersed respiratory supercomplexes and complexes. Furthermore, it is assumed that ATP-synthase (complex V) does not form associations with respiratory enzymes and operates autonomously. Our latest data obtained on mitochondria of etiolated shoots of pea evidence the possibility of physical association between the respiratory supercomplexes and dimeric ATP-synthase. These data have allowed us to reconsider the contemporary concept of the phosphorylation system organization and propose a new subcompartmented oxphosomic model. According to this model, a substantial number of the OXPHOS complexes form oxphosomes, which in a definite stoichiometry include complexes I–V and are located predominantly in the cristae subcompartment of mitochondria in the form of highly organized strings or patches. These suprastructures represent “mini-factories” for ATP production. It is assumed that such an organization (1) contributes to increasing the efficiency of the OXPHOS system operation, (2) involves new levels of activity regulation, and (3) may determine the inner membrane morphology to some extent. The review discusses the proposed model in detail. For a better understanding of the matter, the history of development of concepts concerning the OXPHOS organization with the emphasis on recent contemporary models is briefly considered. The principal experimental data accumulated over the past 40 years, which confirm the validity of the oxphosomic hypothesis, are also provided.
format Article
id doaj-art-38b5e008b3bd49f9b09cff639d4a5a7d
institution Kabale University
issn 2500-3259
language English
publishDate 2021-12-01
publisher Siberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and Breeders
record_format Article
series Вавиловский журнал генетики и селекции
spelling doaj-art-38b5e008b3bd49f9b09cff639d4a5a7d2025-02-01T09:58:10ZengSiberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and BreedersВавиловский журнал генетики и селекции2500-32592021-12-0125777878610.18699/VJ21.0891214The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondriaI. V. Ukolova0Siberian Institute of Plant Physiology and Biochemistry of the Siberian Branch of the Russian Academy of SciencesThe oxidative phosphorylation (OXPHOS) system of mitochondria supports all the vitally important energyconsuming processes in eukaryotic cells, providing them with energy in the form of ATP. OXPHOS enzymes (complexes I–V) are located in the inner mitochondrial membrane, mainly in the cristae subcompartment. At present, there is a large body of data evidencing that the respiratory complexes I, III2 and IV under in vivo conditions can physically interact with each other in diverse stoichiometry, thereby forming supercomplexes. Despite active accumulation of knowledge about the structure of the main supercomplexes of the OXPHOS system, its physical and functional organization in vivo remains unclear. Contemporary models of the OXPHOS system’s organization in the inner membrane of mitochondria are contradictory and presume the existence of either highly organized respiratory strings, or, by contrast, a set of randomly dispersed respiratory supercomplexes and complexes. Furthermore, it is assumed that ATP-synthase (complex V) does not form associations with respiratory enzymes and operates autonomously. Our latest data obtained on mitochondria of etiolated shoots of pea evidence the possibility of physical association between the respiratory supercomplexes and dimeric ATP-synthase. These data have allowed us to reconsider the contemporary concept of the phosphorylation system organization and propose a new subcompartmented oxphosomic model. According to this model, a substantial number of the OXPHOS complexes form oxphosomes, which in a definite stoichiometry include complexes I–V and are located predominantly in the cristae subcompartment of mitochondria in the form of highly organized strings or patches. These suprastructures represent “mini-factories” for ATP production. It is assumed that such an organization (1) contributes to increasing the efficiency of the OXPHOS system operation, (2) involves new levels of activity regulation, and (3) may determine the inner membrane morphology to some extent. The review discusses the proposed model in detail. For a better understanding of the matter, the history of development of concepts concerning the OXPHOS organization with the emphasis on recent contemporary models is briefly considered. The principal experimental data accumulated over the past 40 years, which confirm the validity of the oxphosomic hypothesis, are also provided.https://vavilov.elpub.ru/jour/article/view/3182system of oxidative phosphorylationmitochondriaoxphosomemodels of the oxphos organizationsupercomplexes
spellingShingle I. V. Ukolova
The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria
Вавиловский журнал генетики и селекции
system of oxidative phosphorylation
mitochondria
oxphosome
models of the oxphos organization
supercomplexes
title The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria
title_full The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria
title_fullStr The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria
title_full_unstemmed The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria
title_short The subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria
title_sort subcompartmented oxphosomic model of the phosphorylating system organization in mitochondria
topic system of oxidative phosphorylation
mitochondria
oxphosome
models of the oxphos organization
supercomplexes
url https://vavilov.elpub.ru/jour/article/view/3182
work_keys_str_mv AT ivukolova thesubcompartmentedoxphosomicmodelofthephosphorylatingsystemorganizationinmitochondria
AT ivukolova subcompartmentedoxphosomicmodelofthephosphorylatingsystemorganizationinmitochondria