Results 231 to 240 of about 5,833,753 (257)

The structure of the TOM core complex in the mitochondrial outer membrane

Biological Chemistry, 2020
Abstract In the past three decades, significant advances have been made in providing the biochemical background of TOM (translocase of the outer mitochondrial membrane)-mediated protein translocation into mitochondria. In the light of recent cryoelectron microscopy-derived structures of TOM isolated from Neurospora crassa and ...
Hammad Naveed, Jie Liang, Stephan Nußberger   +2 more
exaly   +4 more sources

Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex

Molecular Cell, 2022
Mutations in PINK1 cause autosomal-recessive Parkinson's disease. Mitochondrial damage results in PINK1 import arrest on the translocase of the outer mitochondrial membrane (TOM) complex, resulting in the activation of its ubiquitin kinase activity by autophosphorylation and initiation of Parkin-dependent mitochondrial clearance.
Mohamed A Eldeeb, Shafqat Rasool, Edward A. Fon   +2 more
exaly   +3 more sources

The TOM complex is involved in the release of superoxide anion from mitochondria

Journal of Bioenergetics and Biomembranes, 2009
Available data indicate that superoxide anion (O(2)(*-) ) is released from mitochondria, but apart from VDAC (voltage dependent anion channel), the proteins involved in its transport across the mitochondrial outer membrane still remain elusive. Using mitochondria of the yeast Saccharomyces cerevisiae mutant depleted of VDAC (Deltapor1 mutant) and the ...
Hanna Kmita, Małgorzata Wojtkowska, Andonis Karachitos   +2 more
exaly   +3 more sources

Annealing synchronizes the TOM complex with Tom7 in a new orientation

Archives of Biochemistry and Biophysics
Annealing is an ideal approach to synchronizing soluble proteins into their minimum-energy states via tandem heating and cooling treatments. Like soluble proteins, many membrane proteins also suffer intrinsic structural flexibility, the major obstacle to high-resolution structural determination.
Xubo Lin, Qing-Tao Shen, Liuyan Yang
exaly   +3 more sources

Cooperation of TOM and TIM23 Complexes during Translocation of Proteins into Mitochondria

Journal of Molecular Biology, 2015
Translocation of the majority of mitochondrial proteins from the cytosol into mitochondria requires the cooperation of TOM and TIM23 complexes in the outer and inner mitochondrial membranes. The molecular mechanisms underlying this cooperation remain largely unknown.
Waegemann, K., Popov-Čeleketić, D., Neupert, W., Azem, A., Mokranjac, D.   +4 more
openaire   +3 more sources

Beyond ER: Regulating TOM-Complex-Mediated Import by Ubx2

Trends in Cell Biology, 2019
Despite the progress in understanding the molecular responses to mitochondrial damage, responses to aberrant accumulation of mitochondrial precursor proteins and mitochondrial import defects remain poorly understood. Recent work (Mårtensson et al., Nature, 2019) has unveiled a pathway similar to endoplasmic-reticulum-associated degradation (ERAD) in ...
Mohamed A, Eldeeb, Emma J, MacDougall, Mohamed A, Ragheb, Edward A, Fon   +3 more
openaire   +2 more sources

The shape of micelles of a complex soap causing the Toms effect

Colloid & Polymer Science, 1983
It is well known that a small addition of some substances to a fluid is the cause of Toms effect. In order to explain this effect various theories have been proposed which take into consideration the shape of microparticles in the additives (macromolecules and soapmicelles). We have investigated the shape and the size of micelles or their aggregates of
J. Myška, Marta Šimečková
openaire   +1 more source

The Transmembrane Segment of Tom20 Is Recognized by Mim1 for Docking to the Mitochondrial TOM Complex

Journal of Molecular Biology, 2008
Mitochondria cannot be made de novo. Mitochondrial biogenesis requires that up to 1000 proteins are imported into mitochondria, and the protein import pathway relies on hetero-oligomeric translocase complexes in both the inner and outer mitochondrial membranes. The translocase in the outer membrane, the TOM complex, is composed of a core complex formed
Joanne M, Hulett, Franziska, Lueder, Nickie C, Chan, Andrew J, Perry, Peter, Wolynec, Vladimir A, Likić, Paul R, Gooley, Trevor, Lithgow   +7 more
openaire   +2 more sources

The Translocase of the Outer Membrane of Mitochondria (TOM complex)

2003
The TOM complex, a multisubunit assembly in the mitochondrial outer membrane, mediates targeting and membrane translocation of virtually all nuclear-encoded mitochondrial preproteins analyzed so far. In the present study the mechanisms by which the TOM complex recognizes different precursor proteins and translocates them across the outer membrane were ...
openaire   +1 more source

The function of Mim1 in the biogenesis of the mitochondrial TOM complex

2008
The translocase of the outer mitochondrial membrane (TOM complex) is the general entry site for newly synthesized proteins into the organelle. The translocase is a multi-subunit complex composed of seven subunits: two receptor proteins, Tom70 and Tom20, and five components which form the core complex, Tom40, Tom22, Tom7, Tom6, and Tom5.
openaire   +1 more source