Structural rearrangements in mRNA upon its binding to human 80S ribosomes revealed by EPR spectroscopy

Structural rearrangements in mRNA upon its binding to human 80S ribosomes revealed by EPR spectroscopy Full article

Journal

Nucleic Acids Research
ISSN: 0305-1048 , E-ISSN: 1362-4962

Output data

Year: 2018, Volume: 46, Number: 2, Pages: 897-904 Pages count : 8 DOI: 10.1093/nar/gkx1136

Authors

Malygin Alexey A. ^1,2 , Graifer Dmitri M. ^1,2 , Meschaninova Maria I. ¹ , Venyaminova Alya G. ¹ , Timofeev Ivan O. ^2,3,4 , Kuzhelev Andrey A. ^2,3,4 , Krumkacheva Olesya A. ^2,3,4 , Fedin Matvey V. ^2,3 , Karpova Galina G. ^1,2 , Bagryanskaya Elena G. ^2,4

Affiliations

1	(Данные Web of science) Inst Chem Biol & Fundamental Med SB RAS, Pr Lavrentjeva 8, Novosibirsk 630090, Russia
2	(Данные Web of science) Novosibirsk State Univ, Pirogova Str 2, Novosibirsk 630090, Russia
3	(Данные Web of science) Int Tomog Ctr SB RAS, Inst Skaya Str 3a, Novosibirsk 630090, Russia
4	(Данные Web of science) NN Vorozhtsov Novosibirsk Inst Organ Chem SB RAS, Pr Lavrentjeva 9, Novosibirsk 630090, Russia

The model mRNA (MR), 11-mer RNA containing two nitroxide spin labels at the 5'-and 3'-terminal nucleotides and prone to form a stable homodimer (MR) 2, was used for Electron Paramagnetic Resonance study of structural rearrangements in mRNA occurring upon its binding to human 80S ribosomes. The formation of two different types of ribosomal complexes with MR was observed. First, there were stable complexes where MR was fixed in the ribosomal mRNA-binding channel by the codon-anticodon interaction(s) with cognate tRNA(s). Second, we for the first time detected complexes assembled without tRNA due to the binding of MR most likely to an exposed peptide of ribosomal protein uS3 away from the mRNA channel. The analysis of interspin distances allowed the conclusion that 80S ribosomes facilitate dissociation of the duplex (MR) 2: the equilibrium between the duplex and the single-stranded MR shifts to MR due to its efficient binding with ribosomes. Furthermore, we observed a significant influence of tRNA bound at the ribosomal exit (E) and/ or aminoacyl (A) sites on the stability of ribosomal complexes. Our findings showed that a part of mRNA bound in the ribosome channel, which is not involved in codon-anticodon interactions, has more degrees of freedom than that interacting with tRNAs.

Malygin A.A. , Graifer D.M. , Meschaninova M.I. , Venyaminova A.G. , Timofeev I.O. , Kuzhelev A.A. , Krumkacheva O.A. , Fedin M.V. , Karpova G.G. , Bagryanskaya E.G.
Structural rearrangements in mRNA upon its binding to human 80S ribosomes revealed by EPR spectroscopy

Nucleic Acids Research. 2018. V.46. N2. P.897-904. DOI: 10.1093/nar/gkx1136 WOS Scopus РИНЦ OpenAlex

Full text from publisher

Published online:	Nov 16, 2017
Published print:	Jan 25, 2018

Web of science:	WOS:000423812300037
Scopus:	2-s2.0-85044640684
Elibrary:	35531377
OpenAlex:	W2769846544

DB	Citing
Web of science	7
Scopus	10
Elibrary	11
OpenAlex	11