Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add filters








Year range
1.
Chinese Journal of Biochemistry and Molecular Biology ; (12): 15-27, 2022.
Article in Chinese | WPRIM | ID: wpr-1015733

ABSTRACT

Mitochondria, originated from the last eukaryotic common ancestor by endosymbiosis, are semi-autonomous double-membrane organelles. The oxidative phosphorylation system consists of five complexes that are coordinately encoded by the nuclear and mitochondrial genomes, and establishes the electron transport chain in the mitochondrial inner membrane, concurrently generating ATP using the proton gradient. The proton-pumping Complex I (NADH:ubiquinone oxidoreductase) is the first, large stand most complicated enzyme required in this process. Complex I is an L-shaped multimeric enzyme harbouring over 40 subunits, one FMN molecule and eight Fe-S clusters. In recent years, biochemical, genetic, proteomic and crysta-structure analyses of Complex I in several model systems have provided valuable insights into its function and biogenesis. This review summarizes our current understanding of Complex I structural modules, assembly pathway and factors, discusses their similarities and distinctions between animals and plants, as well as the evolution of Complex I. And we proposes some potentially important but yet unsolved questions of Complex I. Therefore, this review provides a relevant reference for further comprehensively deepening the function and evolution of mitochondrial Complex I.

2.
Mycobiology ; : 1-12, 2013.
Article in English | WPRIM | ID: wpr-729691

ABSTRACT

Msi1-like (MSIL) proteins, which are eukaryote-specific and contain a series of WD40 repeats, have pleiotropic roles in chromatin assembly, DNA damage repair, and regulation of nutrient/stress-sensing signaling pathways. In the fungal kingdom, the functions of MSIL proteins have been studied most intensively in the budding yeast model Saccharomyces cerevisiae, an ascomycete. Yet their functions are largely unknown in other fungi. Recently, an MSIL protein, Msl1, was discovered and functionally characterized in the pathogenic yeast Cryptococcus neoformans, a basidiomycete. Interestingly, MSIL proteins appear to have redundant and unique roles in both fungi, suggesting that MSIL proteins may have evolutionarily divergent roles in different parts of the fungal kingdom. In this review, we will describe the current findings regarding the role of MSIL proteins in fungi and discuss future directions for research on this topic.


Subject(s)
Ascomycota , Basidiomycota , Chromatin Assembly and Disassembly , Cryptococcus neoformans , DNA Damage , Fungi , Histones , Proteins , Retinoblastoma , Saccharomyces cerevisiae , Saccharomycetales , Yeasts
SELECTION OF CITATIONS
SEARCH DETAIL