Maintenance of protein synthesis reading frame by EF-P and m1G37-tRNA

Howard B. Gamper, Isao Masuda, Milana Frenkel-Morgenstern and Ya-Ming Hou ()
Additional contact information
Howard B. Gamper: Thomas Jefferson University
Isao Masuda: Thomas Jefferson University
Milana Frenkel-Morgenstern: Faculty of Medicine, Bar-Ilan University
Ya-Ming Hou: Thomas Jefferson University

Nature Communications, 2015, vol. 6, issue 1, 1-13

Abstract: Abstract Maintaining the translational reading frame poses difficulty for the ribosome. Slippery mRNA sequences such as CC[C/U]-[C/U], read by isoacceptors of tRNAPro, are highly prone to +1 frameshift (+1FS) errors. Here we show that +1FS errors occur by two mechanisms, a slow mechanism when tRNAPro is stalled in the P-site next to an empty A-site and a fast mechanism during translocation of tRNAPro into the P-site. Suppression of +1FS errors requires the m1G37 methylation of tRNAPro on the 3' side of the anticodon and the translation factor EF-P. Importantly, both m1G37 and EF-P show the strongest suppression effect when CC[C/U]-[C/U] are placed at the second codon of a reading frame. This work demonstrates that maintaining the reading frame immediately after the initiation of translation by the ribosome is an essential aspect of protein synthesis.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms8226 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8226

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms8226

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().