LOVELAND, A.B., Gabriel DEMO and A.A. KOROSTELEV. Cryo-EM of elongating ribosome with EF-Tu center dot GTP elucidates tRNA proofreading. Nature. LONDON: NATURE PUBLISHING GROUP, 2020, vol. 584, No 7822, p. "640"-"+", 24 pp. ISSN 0028-0836. Available from: https://dx.doi.org/10.1038/s41586-020-2447-x.
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Basic information
Original name Cryo-EM of elongating ribosome with EF-Tu center dot GTP elucidates tRNA proofreading
Authors LOVELAND, A.B., Gabriel DEMO (703 Slovakia, guarantor, belonging to the institution) and A.A. KOROSTELEV.
Edition Nature, LONDON, NATURE PUBLISHING GROUP, 2020, 0028-0836.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 49.962
RIV identification code RIV/00216224:14740/20:00118257
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1038/s41586-020-2447-x
UT WoS 000544885800003
Keywords in English AMINOACYL-TRANSFER-RNA; ALLOSTERIC 3-SITE MODEL; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; STRUCTURAL BASIS; PROTEIN L7/12; 70S RIBOSOME; VISUALIZATION; RESOLUTION; HYDROLYSIS
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 24/2/2021 14:55.
Abstract
Ribosomes accurately decode mRNA by proofreading each aminoacyl-tRNA that is delivered by the elongation factor EF-Tu(1). To understand the molecular mechanism of this proofreading step it is necessary to visualize GTP-catalysed elongation, which has remained a challenge(2-4). Here we use time-resolved cryogenic electron microscopy to reveal 33 ribosomal states after the delivery of aminoacyl-tRNA by EF-Tu center dot GTP. Instead of locking cognate tRNA upon initial recognition, the ribosomal decoding centre dynamically monitors codon-anticodon interactions before and after GTP hydrolysis. GTP hydrolysis enables the GTPase domain of EF-Tu to extend away, releasing EF-Tu from tRNA. The 30S subunit then locks cognate tRNA in the decoding centre and rotates, enabling the tRNA to bypass 50S protrusions during accommodation into the peptidyl transferase centre. By contrast, the decoding centre fails to lock near-cognate tRNA, enabling the dissociation of near-cognate tRNA both during initial selection (before GTP hydrolysis) and proofreading (after GTP hydrolysis). These findings reveal structural similarity between ribosomes in initial selection states(5,6)and in proofreading states, which together govern the efficient rejection of incorrect tRNA. Time-resolved cryogenic electron microscopy structures of a ribosome during the delivery of aminoacyl-tRNA by EF-Tu center dot GTP capture 33 ribosomal states, enabling visualization of the initial selection, proofreading and peptidyl transfer stages.
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