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Sökning: WFRF:(Amunts Alexey) > (2020)

  • Resultat 1-9 av 9
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1.
  • Aibara, Shintaro, et al. (författare)
  • Structural basis of mitochondrial translation
  • 2020
  • Ingår i: eLIFE. - 2050-084X. ; 9
  • Tidskriftsartikel (refereegranskat)abstract
    • Translation of mitochondrial messenger RNA (mt-mRNA) is performed by distinct mitoribosomes comprising at least 36 mitochondria-specific proteins. How these mitoribosomal proteins assist in the binding of mt-mRNA and to what extent they are involved in the translocation of transfer RNA (mt-tRNA) is unclear. To visualize the process of translation in human mitochondria, we report similar to 3.0 angstrom resolution structure of the human mitoribosome, including the L7/L12 stalk, and eight structures of its functional complexes with mt-mRNA, mt-tRNAs, recycling factor and additional trans factors. The study reveals a transacting protein module LRPPRC-SLIRP that delivers mt-mRNA to the mitoribosomal small subunit through a dedicated platform formed by the mitochondria-specific protein mS39. Mitoribosomal proteins of the large subunit mL40, mL48, and mL64 coordinate translocation of mt-tRNA. The comparison between those structures shows dynamic interactions between the mitoribosome and its ligands, suggesting a sequential mechanism of conformational changes.
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2.
  • Chen, Ming, et al. (författare)
  • Distinct structural modulation of photosystem I and lipid environment stabilizes its tetrameric assembly
  • 2020
  • Ingår i: Nature Plants. - 2055-026X .- 2055-0278. ; 6:3, s. 314-
  • Tidskriftsartikel (refereegranskat)abstract
    • Photosystem I (PSI) is able to form different oligomeric states across various species. To reveal the structural basis for PSI dimerization and tetramerization, we structurally investigated PSI from the cyanobacterium Anabaena. This revealed a disrupted trimerization domain due to lack of the terminal residues of PsaL in the lumen, which resulted in PSI dimers with loose connections between monomers and weaker energy-coupled chlorophylls than in the trimer. At the dimer surface, specific phospholipids, cofactors and interactions in combination facilitated recruitment of another dimer to form a tetramer. Taken together, the relaxed luminal connections and lipid specificity at the dimer interface account for membrane curvature. PSI tetramer assembly appears to increase the surface area of the thylakoid membrane, which would contribute to PSI crowding. Photosystem I from the cyanobacterium Anabaena has a disrupted trimerization domain resulting in dimers with loose connections between monomers. Phospholipids and cofactors at the dimer surface facilitate further dimerization to form a tetramer.
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3.
  • Itoh, Yuzuru, et al. (författare)
  • Analysis of translating mitoribosome reveals functional characteristics of translation in mitochondria of fungi
  • 2020
  • Ingår i: Nature Communications. - 2041-1723 .- 2041-1723. ; 11:1
  • Tidskriftsartikel (refereegranskat)abstract
    • Mitoribosomes are specialized protein synthesis machineries in mitochondria. However, how mRNA binds to its dedicated channel, and tRNA moves as the mitoribosomal subunit rotate with respect to each other is not understood. We report models of the translating fungal mitoribosome with mRNA, tRNA and nascent polypeptide, as well as an assembly intermediate. Nicotinamide adenine dinucleotide (NAD) is found in the central protuberance of the large subunit, and the ATPase inhibitory factor 1 (IF1) in the small subunit. The models of the active mitoribosome explain how mRNA binds through a dedicated protein platform on the small subunit, tRNA is translocated with the help of the protein mL108, bridging it with L1 stalk on the large subunit, and nascent polypeptide paths through a newly shaped exit tunnel involving a series of structural rearrangements. An assembly intermediate is modeled with the maturation factor Atp25, providing insight into the biogenesis of the mitoribosomal large subunit and translation regulation.
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4.
  • Khawaja, Anas, et al. (författare)
  • Distinct pre-initiation steps in human mitochondrial translation
  • 2020
  • Ingår i: Nature Communications. - 2041-1723 .- 2041-1723. ; 11:1
  • Tidskriftsartikel (refereegranskat)abstract
    • Translation initiation in human mitochondria relies upon specialized mitoribosomes and initiation factors, mtIF2 and mtIF3, which have diverged from their bacterial counterparts. Here we report two distinct mitochondrial pre-initiation assembly steps involving those factors. Single-particle cryo-EM revealed that in the first step, interactions between mitochondria-specific protein mS37 and mtIF3 keep the small mitoribosomal subunit in a conformation favorable for a subsequent accommodation of mtIF2 in the second step. Combination with fluorescence cross-correlation spectroscopy analyses suggests that mtIF3 promotes complex assembly without mRNA or initiator tRNA binding, where exclusion is achieved by the N-terminal and C-terminal domains of mtIF3. Finally, the association of large mitoribosomal subunit is required for initiator tRNA and leaderless mRNA recruitment to form a stable initiation complex. These data reveal fundamental aspects of mammalian protein synthesis that are specific to mitochondria.
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5.
  • Kock Flygaard, Rasmus, et al. (författare)
  • Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization
  • 2020
  • Ingår i: Nature Communications. - 2041-1723 .- 2041-1723. ; 11:1
  • Tidskriftsartikel (refereegranskat)abstract
    • Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 angstrom resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.
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6.
  • Perez Boerema, Annemarie, 1991- (författare)
  • Cryo-EM Studies of Macromolecular Complexes from Photosynthetic Organisms
  • 2020
  • Doktorsavhandling (övrigt vetenskapligt)abstract
    • Plants, algae, and cyanobacteria convert light energy into chemical energy through the process of photosynthesis, fueling the planet and making life as we know it possible. Photosystem I (PSI) is one of the main photosynthetic complexes, responsible for this process. PSI uses the energy of light to transfer electrons from the soluble electron carrier plastocyanin, on the lumenal site of the thylakoid membrane, to ferrodoxin, on the stromal site of the membrane. Thus, playing a key role in the light dependent reactions. In order to survive many photosynthetic organisms need to be able to adapt to fluctuations in light and have adapted their photosynthetic machinery accordingly. In recent years many advances have been made in electron cryo-microscopy, making it possible to visualize many previously elusive photosynthetic complexes. This has brought a wealth of information on the structural adaptations of PSI.In plants and algae, PSI is hosted by the chloroplast, a specialized organelle that houses the photosynthetic reactions. In the chloroplast, key components of PSI are synthesized by the chloroplasts own translation machinery: the chloroplast ribosome. Translation in the chloroplast is remarkable as it has to synchronize translation in two different genetic compartments as well as adapt to fluctuations in light. A glimpse of how this machinery has evolved to be able to fulfill all of these duties can be obtained from its three dimensional structure and its chloroplast specific features. However, despite all this structural information providing valuable clues as to the functioning of these systems, there are still many aspects of how they play a role that still remain unknown.
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7.
  • Perez-Boerema, Annemarie, et al. (författare)
  • Structure of a minimal photosystem I from the green alga Dunaliella salina
  • 2020
  • Ingår i: Nature plants. - 2055-026X .- 2055-0278. ; 6:3, s. 321-327
  • Tidskriftsartikel (refereegranskat)abstract
    • Solar energy harnessed by oxygenic photosynthesis supports most of the life forms on Earth. In eukaryotes, photosynthesis occurs in chloroplasts and is achieved by membrane-embedded macromolecular complexes that contain core and peripheral antennae with multiple pigments. The structure of photosystem I (PSI) comprises the core and light-harvesting (LHCI) complexes, which together form PSI-LHCI. Here we determined the structure of PSI-LHCI from the salt-tolerant green alga Dunaliella salina using X-ray crystallography and electron cryo-microscopy. Our results reveal a previously undescribed configuration of the PSI core. It is composed of only 7 subunits, compared with 14-16 subunits in plants and the alga Chlamydomonas reinhardtii, and forms the smallest known PSI. The LHCI is poorly conserved at the sequence level and binds to pigments that form new energy pathways, and the interactions between the individual Lhca1-4 proteins are weakened. Overall, the data indicate the PSI of D. salina represents a different type of the molecular organization that provides important information for reconstructing the plasticity and evolution of PSI. The photosystem I light-harvesting complex from the salt-tolerant green alga Dunaliella salina has a core configuration composed of only seven subunits. This unusual molecular organization could inform the reconstruction of photosystem evolution.
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8.
  • Tobiasson, Victor, et al. (författare)
  • Ciliate mitoribosome illuminates evolutionary steps of mitochondrial translation
  • 2020
  • Ingår i: eLIFE. - 2050-084X. ; 9
  • Tidskriftsartikel (refereegranskat)abstract
    • To understand the steps involved in the evolution of translation, we used Tetrahymena thermophila, a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ribosome (mitoribosome) using cryo-EM. The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit, while the large subunit lacks 5S rRNA. The structure also shows that the small subunit head is constrained, tRNA binding sites are formed by mitochondria-specific protein elements, conserved protein bS1 is excluded, and bacterial RNA polymerase binding site is blocked. We provide evidence for anintrinsic protein targeting system through visualization of mitochondria-specific mL105 by the exit tunnel that would facilitate the recruitment of a nascent polypeptide. Functional protein uS3m is encoded by three complementary genes from the nucleus and mitochondrion, establishing a link between genetic drift and mitochondrial translation. Finally, we reannotated nine open reading frames in the mitochondrial genome that code for mitoribosomal proteins.
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  • Resultat 1-9 av 9

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