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  • 1
    In: Nucleic Acids Research, Oxford University Press (OUP), Vol. 51, No. 16 ( 2023-09-08), p. 8691-8710
    Abstract: 5-Methyluridine (m5U) is one of the most abundant RNA modifications found in cytosolic tRNA. tRNA methyltransferase 2 homolog A (hTRMT2A) is the dedicated mammalian enzyme for m5U formation at tRNA position 54. However, its RNA binding specificity and functional role in the cell are not well understood. Here we dissected structural and sequence requirements for binding and methylation of its RNA targets. Specificity of tRNA modification by hTRMT2A is achieved by a combination of modest binding preference and presence of a uridine in position 54 of tRNAs. Mutational analysis together with cross-linking experiments identified a large hTRMT2A–tRNA binding surface. Furthermore, complementing hTRMT2A interactome studies revealed that hTRMT2A interacts with proteins involved in RNA biogenesis. Finally, we addressed the question of the importance of hTRMT2A function by showing that its knockdown reduces translation fidelity. These findings extend the role of hTRMT2A beyond tRNA modification towards a role in translation.
    Type of Medium: Online Resource
    ISSN: 0305-1048 , 1362-4962
    RVK:
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2023
    detail.hit.zdb_id: 1472175-2
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    American Association for the Advancement of Science (AAAS) ; 2009
    In:  Science Vol. 324, No. 5930 ( 2009-05-22), p. 1087-1091
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 324, No. 5930 ( 2009-05-22), p. 1087-1091
    Abstract: CRM1 mediates nuclear export of numerous unrelated cargoes, which may carry a short leucine-rich nuclear export signal or export signatures that include folded domains. How CRM1 recognizes such a variety of cargoes has been unknown up to this point. Here we present the crystal structure of the SPN1⋅CRM1⋅RanGTP export complex at 2.5 angstrom resolution (where SPN1 is snurportin1 and RanGTP is guanosine 5′ triphosphate–bound Ran). SPN1 is a nuclear import adapter for cytoplasmically assembled, m 3 G-capped spliceosomal U snRNPs (small nuclear ribonucleoproteins). The structure shows how CRM1 can specifically return the cargo-free form of SPN1 to the cytoplasm. The extensive contact area includes five hydrophobic residues at the SPN1 amino terminus that dock into a hydrophobic cleft of CRM1, as well as numerous hydrophilic contacts of CRM1 to m 3 G cap-binding domain and carboxyl-terminal residues of SPN1. The structure suggests that RanGTP promotes cargo-binding to CRM1 solely through long-range conformational changes in the exportin.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
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    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2009
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
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  • 3
    Online Resource
    Online Resource
    American Society for Microbiology ; 2013
    In:  Applied and Environmental Microbiology Vol. 79, No. 5 ( 2013-03), p. 1739-1742
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 79, No. 5 ( 2013-03), p. 1739-1742
    Abstract: Eight Staphylococcus aureus isolates collected from 117 wild boars were characterized and compared to livestock isolates. They belonged to sequence types ST133, ST425, and the new type ST1643. The spa types were t1181, t6782, and the new types t6384, t6385, and t6386. Antimicrobial susceptibility testing and microarray-based genotyping confirmed the absence of important virulence/resistance genes.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
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    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2013
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2009
    In:  Nucleic Acids Research Vol. 37, No. 12 ( 2009-7), p. 3865-3877
    In: Nucleic Acids Research, Oxford University Press (OUP), Vol. 37, No. 12 ( 2009-7), p. 3865-3877
    Type of Medium: Online Resource
    ISSN: 1362-4962 , 0305-1048
    RVK:
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2009
    detail.hit.zdb_id: 1472175-2
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2022
    In:  Journal of Mammalogy Vol. 103, No. 2 ( 2022-04-11), p. 471-480
    In: Journal of Mammalogy, Oxford University Press (OUP), Vol. 103, No. 2 ( 2022-04-11), p. 471-480
    Abstract: Common hamsters (Cricetus cricetus) are hibernators that rely both on body fat reserves and food stores for the winter period. They face an ongoing population decline in most parts of their distribution and recently were classified as critically endangered. Knowledge on individual body fat proportions in this species is of particular interest for conservation, because it could contribute to better understand the high plasticity in overwintering strategies, overwinter mortality rates, individual variations in reproductive output, and give information on the animals’ health state. To calculate body fat proportions, we validated a method that can be applied in the field without the use of anesthesia. To develop this method, we first analyzed the body fat in carcasses of common hamsters using Soxhlet extractions and measured four morphometric parameters (body mass, head length, tibia length, foot length). The morphometric measurements were then integrated in a linear regression model to predict body fat proportions based on the measured values. The morphometric variables yielded an explained variance (adjusted R2) of 96.42% and body fat proportions were predicted with a mean absolute error of 1.27 ± 0.11% from measured values. We applied the model to predict body fat for available field data, which consistently produced reliable values. By measuring the four morphometric parameters and following the provided instructions, body fat proportions can be reliably and noninvasively estimated in captive or free-ranging common hamsters. Furthermore, the method could be applicable to other rodents after species-specific validation.
    Type of Medium: Online Resource
    ISSN: 0022-2372 , 1545-1542
    RVK:
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2022
    detail.hit.zdb_id: 2066602-0
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 2013
    In:  Proceedings of the National Academy of Sciences Vol. 110, No. 3 ( 2013-01-15), p. 960-965
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 110, No. 3 ( 2013-01-15), p. 960-965
    Abstract: In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-β superfamily termed importins and exportins. The highly versatile exportin chromosome region maintenance 1 (CRM1) is essential for nuclear depletion of numerous structurally and functionally unrelated protein and ribonucleoprotein cargoes. CRM1 has been shown to adopt a toroidal structure in several functional transport complexes and was thought to maintain this conformation throughout the entire nucleocytoplasmic transport cycle. We solved crystal structures of free CRM1 from the thermophilic eukaryote Chaetomium thermophilum . Surprisingly, unbound CRM1 exhibits an overall extended and pitched superhelical conformation. The two regulatory regions, namely the acidic loop and the C-terminal α-helix, are dramatically repositioned in free CRM1 in comparison with the ternary CRM1–Ran–Snurportin1 export complex. Single-particle EM analysis demonstrates that, in a noncrystalline environment, free CRM1 exists in equilibrium between extended, superhelical and compact, ring-like conformations. Molecular dynamics simulations show that the C-terminal helix plays an important role in regulating the transition from an extended to a compact conformation and reveal how the binding site for nuclear export signals of cargoes is modulated by different CRM1 conformations. Combining these results, we propose a model for the cooperativity of CRM1 export complex assembly involving the long-range allosteric communication between the distant binding sites of GTP-bound Ran and cargo.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
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    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2013
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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