Abstract:
: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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Malygin AA,Graifer DM,Meschaninova MI,Venyaminova AG,Timofeev IO,Kuzhelev AA,Krumkacheva OA,Fedin MV,Karpova GG,Bagryanskaya EGdoi
10.1093/nar/gkx1136subject
Has Abstractpub_date
2018-01-25 00:00:00pages
897-904issue
2eissn
0305-1048issn
1362-4962pii
4634009journal_volume
46pub_type
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