By using a combination of biochemistry and genetics, in this issue of Molecular CellIeva et al. (2014) uncover an unexpected role for Mgr2 of the mitochondrial TIM23 translocon as a gatekeeper in the release of membrane proteins from the translocon.
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Structure prediction analysis of human core TIM23 complex reveals conservation of the protein translocation mechanism.
FEBS Open Bio
October 2024
IMol Polish Academy of Sciences, Warsaw, Poland.
The majority of mitochondrial proteins are encoded in the nucleus, translated on cytosolic ribosomes, and subsequently targeted to the mitochondrial surface. Their further import into the organelle is facilitated by highly specialized protein translocases. Mitochondrial precursor proteins that are destined to the mitochondrial matrix and, to some extent, the inner membrane, utilize translocase of the inner membrane (TIM23).
View Article and Find Full Text PDFIdentification of factors limiting the allotopic production of the Cox2 subunit of yeast cytochrome c oxidase.
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June 2024
Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Apartado Postal 70-243, 04510 D.F. (Mexico), México.
Mitochondrial genes can be artificially relocalized in the nuclear genome in a process known as allotopic expression, such is the case of the mitochondrial cox2 gene, encoding subunit II of cytochrome c oxidase (CcO). In yeast, cox2 can be allotopically expressed and is able to restore respiratory growth of a cox2-null mutant if the Cox2 subunit carries the W56R substitution within the first transmembrane stretch. However, the COX2W56R strain exhibits reduced growth rates and lower steady-state CcO levels when compared to wild-type yeast.
View Article and Find Full Text PDFMolecular pathway of mitochondrial preprotein import through the TOM-TIM23 supercomplex.
Nat Struct Mol Biol
December 2023
State Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing, China.
Over half of mitochondrial proteins are imported from the cytosol via the pre-sequence pathway, controlled by the TOM complex in the outer membrane and the TIM23 complex in the inner membrane. The mechanisms through which proteins are translocated via the TOM and TIM23 complexes remain unclear. Here we report the assembly of the active TOM-TIM23 supercomplex of Saccharomyces cerevisiae with translocating polypeptide substrates.
View Article and Find Full Text PDFStructural basis of mitochondrial protein import by the TIM23 complex.
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September 2023
Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA.
Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope. Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel.
View Article and Find Full Text PDFFirst Report of Meloidogyne graminicola on Tomato (Solanum lycopersicum) in Hainan of China.
Plant Dis
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Bio-Agriculture Institute of Shaanxi, Shaanxi Key Laboratory of Plant Nematology, xian, Shaanxi, China;
Article Synopsis
- In Hainan province, Southern China, a tomato crop (cv. Jinsheng) faced yellowing leaves and root galls due to a nematode infestation identified as Meloidogyne graminicola in March 2021.
- Morphological analysis of the nematodes revealed distinct characteristics of both female and juvenile stages, matching descriptions from the original scientific literature.
- DNA extraction and species identification were successfully conducted using specific primers, confirming the presence of M. graminicola through amplification of a 369 bp DNA fragment.
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