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Biomolecules
Special Issues
Mitochondrial Proteins: From Import and Biogenesis to Complex Functional Network
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Mitochondrial Proteins: From Import and Biogenesis to Complex Functional Network

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins, Nucleic Acids and Carbohydrates".

Deadline for manuscript submissions: 30 June 2025 | Viewed by 6926

Special Issue Editor

Dr. Venkatesh Sundararajan

E-Mail Website
Guest Editor
Department of Physiology and Pharmacology, Robert C. Byrd Health Sciences Center, School of Medicine, West Virginia University, Morgantown, WV 26506, USA
Interests: mitochondria; protein quality control; Lon protease; oxidative stress; metabolism; cardiotoxicity; myocardial infarction; mtDNA; cardiovascular disease; cancer

Special Issue Information

Dear Colleagues,

We know that only ~1% of mitochondrial proteins are encoded by mtDNA, and the rest of ~99% are encoded by nuclear DNA and imported into mitochondria through a regulated process, which is critical for optimal cellular function. In addition, mitochondria are not only energy-producing factories but also play vital roles in other subsidiary functions, such as calcium homeostasis, cellular signaling, regulation of heme, steroid, nucleotide, fatty acid synthesis, and apoptosis, to name a few. Therefore, understanding the role of mitochondrial proteins and their contribution to mitochondrial function is of utmost importance as most human diseases are associated with some form of mitochondrial dysfunction. Furthermore, such proteins involve various roles ranging from mitochondrial import and biogenesis to a complex functional network. Therefore, we believe that studying and understanding these mitochondrial proteins is of utmost importance in developing novel therapeutic strategies and tools to target them in human diseases. Thus, I welcome you to contribute to this Special Issue with original or review articles dealing with such mitochondrial proteins to take a step forward in targeting mitochondria in human diseases.

Dr. Venkatesh Sundararajan
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • mitochondrial proteins
  • import
  • biogenesis
  • metabolism
  • functional network
  • oxidative stress
  • small molecules
  • mitochondrial protein quality control
  • mitophagy

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Published Papers (2 papers)

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Research

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23 pages, 2393 KiB  
Article
Salutary Effects of Overexpression of Rsm22, an Assembly Factor for the Mitochondrial Ribosome, on Frataxin/Yfh1 Depletion Phenotypes in Saccharomyces cerevisiae
by Ashutosh K. Pandey, Pratibha Singh, Jayashree Pain, Andrew Dancis and Debkumar Pain
Biomolecules 2025, 15(6), 785; https://doi.org/10.3390/biom15060785 - 28 May 2025
Viewed by 223
Abstract
Frataxin is a component of the iron–sulfur (Fe-S) cluster assembly complex in mitochondria, and deficiency is associated with Friedreich ataxia (FA). The yeast homolog Yfh1 resembles and cross-complements with its human equivalent, and frataxin bypass scenarios are of particular interest because they may [...] Read more.
Frataxin is a component of the iron–sulfur (Fe-S) cluster assembly complex in mitochondria, and deficiency is associated with Friedreich ataxia (FA). The yeast homolog Yfh1 resembles and cross-complements with its human equivalent, and frataxin bypass scenarios are of particular interest because they may point to strategies for treating FA. Here, we describe frataxin/Yfh1 bypass by overexpression of Rsm22, an assembly factor for the mitochondrial ribosome. Rsm22 overexpression in Yfh1-depleted yeast cells restored critical processes in mitochondria, including Fe-S cluster assembly, lipoic acid synthesis, iron homeostasis, and heme synthesis, to a significant extent. Formation of cytoplasmic Fe-S proteins was also restored, suggesting recovery of the mitochondrial ability to generate the (Fe-S)int intermediate that is exported from mitochondria and is utilized for cytoplasmic Fe-S cluster assembly. Importantly, an essential component of the mitochondrial iron–sulfur cluster machinery, namely ferredoxin, was virtually absent in mitochondria lacking Yfh1, but it was recovered with Rsm22 overexpression. Interestingly, ferredoxin overexpression could offset some of the effects of Yfh1 depletion. Ferredoxin has recently been shown to bind to the cysteine desulfurase protein Nfs1 at the same site as Yfh1, in a conserved arginine patch on Nfs1, such that ferredoxin binding at this site may confer frataxin-bypass activity. Full article
(This article belongs to the Special Issue Mitochondrial Proteins: From Import and Biogenesis to Complex Functional Network)
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Review

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16 pages, 1081 KiB  
Review
Electrophilic Aldehyde 4-Hydroxy-2-Nonenal Mediated Signaling and Mitochondrial Dysfunction
by Sudha Sharma, Papori Sharma, Tara Bailey, Susmita Bhattarai, Utsab Subedi, Chloe Miller, Hosne Ara, Srivatsan Kidambi, Hong Sun, Manikandan Panchatcharam and Sumitra Miriyala
Biomolecules 2022, 12(11), 1555; https://doi.org/10.3390/biom12111555 - 25 Oct 2022
Cited by 38 | Viewed by 5817
Abstract
Reactive oxygen species (ROS), a by-product of aerobic life, are highly reactive molecules with unpaired electrons. The excess of ROS leads to oxidative stress, instigating the peroxidation of polyunsaturated fatty acids (PUFA) in the lipid membrane through a free radical chain reaction and [...] Read more.
Reactive oxygen species (ROS), a by-product of aerobic life, are highly reactive molecules with unpaired electrons. The excess of ROS leads to oxidative stress, instigating the peroxidation of polyunsaturated fatty acids (PUFA) in the lipid membrane through a free radical chain reaction and the formation of the most bioactive aldehyde, known as 4-hydroxynonenal (4-HNE). 4-HNE functions as a signaling molecule and toxic product and acts mainly by forming covalent adducts with nucleophilic functional groups in proteins, nucleic acids, and lipids. The mitochondria have been implicated as a site for 4-HNE generation and adduction. Several studies clarified how 4-HNE affects the mitochondria’s functions, including bioenergetics, calcium homeostasis, and mitochondrial dynamics. Our research group has shown that 4-HNE activates mitochondria apoptosis-inducing factor (AIFM2) translocation and facilitates apoptosis in mice and human heart tissue during anti-cancer treatment. Recently, we demonstrated that a deficiency of SOD2 in the conditional-specific cardiac knockout mouse increases ROS, and subsequent production of 4-HNE inside mitochondria leads to the adduction of several mitochondrial respiratory chain complex proteins. Moreover, we highlighted the physiological functions of HNE and discussed their relevance in human pathophysiology and current discoveries concerning 4-HNE effects on mitochondria. Full article
(This article belongs to the Special Issue Mitochondrial Proteins: From Import and Biogenesis to Complex Functional Network)
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