Review
Biochemistry & Molecular Biology
Eleanor Dickson-Murray, Kenza Nedara, Nazanine Modjtahedi, Kostas Tokatlidis
Summary: Mitochondrial proteins, mostly encoded by nuclear genes, must be precisely targeted and sorted within mitochondria. Protein translocases facilitate this process, with the main import pathway for the intermembrane space chemically modifying imported proteins by introducing disulfide bonds. Mia40 is a key component in this pathway, regulated by redox processes, and plays a crucial role in trapping folded precursors in the intermembrane space.
Article
Cell Biology
Esra Peker, Konstantin Weiss, Jiyao Song, Christine Zarges, Sarah Gerlich, Volker Boehm, Aleksandra Trifunovic, Thomas Langer, Niels H. Gehring, Thomas Becker, Jan Riemer
Summary: Peker et al. discovered a two-step import pathway that allows proteins to be localized to both the matrix and IMS. Weak targeting signals enable proteins to form stabilizing disulfide bonds in the IMS before being imported into the matrix. This pathway enables the monitoring of import activity in both compartments. The study found that NDUFAF8, a factor involved in complex I assembly, follows this two-step import pathway, and its import is regulated by proteases to ensure proper function.
JOURNAL OF CELL BIOLOGY
(2023)
Review
Biochemistry & Molecular Biology
Ruairidh Edwards, Ross Eaglesfield, Kostas Tokatlidis
Summary: The mitochondrial intermembrane space (IMS) is a narrow sub-mitochondrial compartment with diverse protein import mechanisms. IMS proteins do not require energy to cross the outer mitochondrial membrane, unlike import into the matrix or inner membrane. Many IMS proteins are associated with human diseases, highlighting the importance of understanding their normal function and localization in the IMS.
Review
Biochemistry & Molecular Biology
Ulfat Mohd Hanif Sayyed, Radhakrishnan Mahalakshmi
Summary: The article discusses the unique properties of the human mitochondrial outer membrane and the importance of the TOM complex. It highlights the recent research progress and the potential impact on alleviating human diseases.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Article
Multidisciplinary Sciences
Qingqing Sun, Xueli Cao, Zihe Liu, Chuanjing An, Jinglei Hu, Yue Wang, Meiyu Qiao, Teng Gao, Wenzhen Cheng, Yi Zhang, Yue Feng, Hongbo Gao
Summary: Chloroplast division involves complex protein interactions, with PDV1 playing a crucial role in stabilizing PARC6. Under light conditions, reduction of a disulfide bond within PARC6 promotes its interaction with PDV1, ultimately leading to chloroplast division. Magnesium ions also enhance PARC6 dimerization, further contributing to the regulation of chloroplast division.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2023)
Article
Multidisciplinary Sciences
Qingqing Sun, Xueli Cao, Zihe Liu, Chuanjing An, Jinglei Hu, Yue Wang, Meiyu Qiao, Teng Gao, Wenzhen Cheng, Yi Zhang, Yue Feng, Hongbo Gao
Summary: Chloroplast division requires the coordination of protein complexes from stroma to cytosol. The interaction between PDV1 and PARC6, crucial for chloroplast division, is regulated by intramolecular disulfide bond formation in PARC6, which can be reduced by light exposure. Additionally, magnesium ions, which increase in chloroplasts upon light exposure, promote PARC6 dimerization.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2023)
Article
Biology
Marcel G. Genge, Shalini Roy Chowdhury, Vit Dohnalek, Kaori Yunoki, Takashi Hirashima, Toshiya Endo, Pavel Dolezal, Dejana Mokranjac
Summary: This study reveals the coordination mechanism of translocation of proteins across mitochondrial membranes, and finds that both the core and PBD domains of Tim50 play essential roles in this process.
LIFE SCIENCE ALLIANCE
(2023)
Review
Biochemistry & Molecular Biology
Hasan Al-Habib, Margaret Ashcroft
Summary: Mitochondria play a crucial role in cellular physiology by regulating various functions such as respiration, bioenergetics, biosynthesis, signaling, and transcription. Dysfunction in mitochondria can lead to the pathology of diseases, including mitochondrial disease and cancer. Import pathways and targeting mechanisms are essential for transporting nuclear-encoded mitochondrial proteins critical for the organelle's functions.
BIOCHEMICAL SOCIETY TRANSACTIONS
(2021)
Article
Biochemistry & Molecular Biology
Danyun Zhang, Owen R. Dailey, Daniel J. Simon, Kamilah Roca-Datzer, Yasaman Jami-Alahmadi, Mikayla S. Hennen, James A. Wohlschlegel, Carla M. Koehler, Deepa Dabir
Summary: Yeast utilizes the MIA pathway to maintain redox-regulated import of cysteine-rich precursors, with Aim32 identified as a key protein interacting with sulfhydryl oxidase Erv1. Aim32 interacts with multiple proteins and plays a role in regulating the oxidation state of mitochondrial proteins.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Review
Physiology
Kyle B. Heine, Hailey A. Parry, Wendy R. Hood
Summary: Our understanding of variation in mitochondrial performance is still limited. The structure of the inner mitochondrial membrane plays a crucial role in ATP production through oxidative phosphorylation. Changes in the morphology and density of the inner mitochondrial membrane can affect ATP synthesis. This review explores the association between ATP synthases, inner mitochondrial membrane density, and mitochondrial density in impacting ATP production by mitochondria, as well as the potential constraints on ATP production due to increased membrane density.
AMERICAN JOURNAL OF PHYSIOLOGY-REGULATORY INTEGRATIVE AND COMPARATIVE PHYSIOLOGY
(2023)
Review
Biochemistry & Molecular Biology
Jakob D. Busch, Laura F. Fielden, Nikolaus Pfanner, Nils Wiedemann
Summary: Biogenesis of mitochondria involves the import of numerous precursor proteins across the mitochondrial membranes. Different import pathways exist, ranging from presequence-directed pathway to pathways using internal or carboxy-terminal targeting signals. Recent studies have revealed the structural organization of membrane-embedded preprotein translocases and their dynamic interactions with other cellular machineries. These insights provide valuable knowledge about the mechanisms of mitochondrial protein import.
Article
Biochemistry & Molecular Biology
Silja Lucia Salscheider, Sarah Gerlich, Alfredo Cabrera-Orefice, Esra Peker, Robin Alexander Rothemann, Lena Maria Murschall, Yannik Finger, Karolina Szczepanowska, Zeinab Alsadat Ahmadi, Sergio Guerrero-Castillo, Alican Erdogan, Mark Becker, Muna Ali, Markus Habich, Carmelina Petrungaro, Nele Burdina, Guenter Schwarz, Merlin Klussmann, Ines Neundorf, David A. Stroud, Michael T. Ryan, Aleksandra Trifunovic, Ulrich Brandt, Jan Riemer
Summary: The study shows that AIFM1 and MIA40/CHCHD4 cooperate beyond the import of MIA40/CHCHD4 and form a stable complex in vitro, in different cell lines, and in tissues. AIFM1 serves two overlapping functions, importing MIA40/CHCHD4 and constituting an integral part of the disulfide relay.
Article
Cell Biology
Marcel Morgenstern, Christian D. Peikert, Philipp Luebbert, Ida Suppanz, Cinzia Klemm, Oliver Alka, Conny Steiert, Nataliia Naumenko, Alexander Schendzielorz, Laura Melchionda, Wignand W. D. Muehlhaeuser, Bettina Knapp, Jakob D. Busch, Sebastian B. Stiller, Stefan Dannenmaier, Caroline Lindau, Mariya Licheva, Christopher Eickhorst, Riccardo Galbusera, Ralf M. Zerbes, Michael T. Ryan, Claudine Kraft, Vera Kozjak-Pavlovic, Friedel Drepper, Sven Dennerlein, Silke Oeljeklaus, Nikolaus Pfanner, Nils Wiedemann, Bettina Warscheid
Summary: Researchers have classified and identified human mitochondrial proteins, establishing a high-confidence mitochondrial proteome containing over 1,100 proteins, which account for 7% of cellular proteins and are linked to various diseases.
Article
Biochemistry & Molecular Biology
Charles Ricordel, Laura Chaillot, Alice Blondel, Jerome Archambeau, Florence Jouan, Audrey Mouche, Marie Tiercin, Agnes Burel, Herve Lena, Benoit Desrues, Thierry Guillaudeux, Remy Pedeux
Summary: ING2 is a tumor suppressor gene involved in key biological functions, it can be imported into mitochondria to participate in new biological functions. Its import into the inner mitochondrial fraction is redox-sensitive and modulated by 14-3-3 eta protein expression. ING2 is essential for maintaining mitochondrial ultrastructure integrity and interacts with mtDNA through TFAM.
Article
Biology
Barbara Uszczynska-Ratajczak, Sreedevi Sugunan, Monika Kwiatkowska, Maciej Migdal, Silvia Carbonell-Sala, Anna Sokol, Cecilia L. Winata, Agnieszka Chacinska
Summary: Most mitochondrial proteins are encoded by nuclear genes, synthesized in the cytosol, and targeted into the organelle. The presence of nuclear-encoded mRNA5 in the mitochondrial fraction confirms that large proteins with specific properties, like transmembrane domains, are predominantly encoded. Under proteostatic stress conditions, the population of transcripts on the mitochondrial surface is further restricted, allowing only the largest and most evolutionarily conserved proteins to be synthesized there.
LIFE SCIENCE ALLIANCE
(2022)
