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GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner

Mitkevich, Vladimir A. ; Shyp, Viktoriya ; Petrushanko, Irina Yu ; Soosaar, Aksel ; Atkinson, Gemma C. LU ; Tenson, Tanel ; Makarov, Alexander A. and Hauryliuk, Vasili LU orcid (2012) In Scientific Reports 2. p.1-6
Abstract

Translational GTPases (trGTPases) are involved in all four stages of protein biosynthesis: initiation, elongation, termination and ribosome recycling. The trGTPases Initiation Factor 2 (IF2) and Elongation Factor G (EF-G) respectively orchestrate initiation complex formation and translocation of the peptidyl-tRNA:mRNA complex through the bacterial ribosome. The ribosome regulates the GTPase cycle and efficiently discriminates between the GDP-and GTP-bound forms of these proteins. Using Isothermal Titration Calorimetry, we have investigated interactions of IF2 and EF-G with the sarcin-ricin loop of the 23S rRNA, a crucial element of the GTPase-associated center of the ribosome. We show that binding of IF2 and EF-G to a 27 nucleotide RNA... (More)

Translational GTPases (trGTPases) are involved in all four stages of protein biosynthesis: initiation, elongation, termination and ribosome recycling. The trGTPases Initiation Factor 2 (IF2) and Elongation Factor G (EF-G) respectively orchestrate initiation complex formation and translocation of the peptidyl-tRNA:mRNA complex through the bacterial ribosome. The ribosome regulates the GTPase cycle and efficiently discriminates between the GDP-and GTP-bound forms of these proteins. Using Isothermal Titration Calorimetry, we have investigated interactions of IF2 and EF-G with the sarcin-ricin loop of the 23S rRNA, a crucial element of the GTPase-associated center of the ribosome. We show that binding of IF2 and EF-G to a 27 nucleotide RNA fragment mimicking the sarcin-ricin loop is mutually exclusive with that of GDP, but not of GTP, providing a mechanism for destabilization of the ribosome-bound GDP forms of translational GTPases.

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author
; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
Scientific Reports
volume
2
article number
843
pages
1 - 6
publisher
Nature Publishing Group
external identifiers
  • pmid:23150791
  • scopus:84869198253
ISSN
2045-2322
DOI
10.1038/srep00843
language
English
LU publication?
no
additional info
Funding Information: We are grateful to Pohl Milon for helpful discussions. This work was supported by the Presidium of the Russian Academy of Sciences (Program Molecular and Cellular Biology to AAM); Estonian Science Foundation grants (grant numbers 7616, 9012 to VH, 6768 to TT, and 9020 to GCA); the European Social Fund through Estonian Science Foundation grants (grant number MJD99 Mobilitas to GCA); the Russian Foundation for Basic Research (grant number 10-04-01746-a to VAM); European Regional Development Fund through the Center of Excellence in Chemical Biology (VH and TT) and SA Archimedes PhD studies and DoRa6 programme grants (VS). Funding for open access charge: European Regional Development Fund through the Center of Excellence in Chemical Biology. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.
id
458d805e-c54e-4346-ba86-4c83ef662c86
date added to LUP
2021-09-24 20:48:43
date last changed
2024-01-05 16:28:54
@article{458d805e-c54e-4346-ba86-4c83ef662c86,
  abstract     = {{<p>Translational GTPases (trGTPases) are involved in all four stages of protein biosynthesis: initiation, elongation, termination and ribosome recycling. The trGTPases Initiation Factor 2 (IF2) and Elongation Factor G (EF-G) respectively orchestrate initiation complex formation and translocation of the peptidyl-tRNA:mRNA complex through the bacterial ribosome. The ribosome regulates the GTPase cycle and efficiently discriminates between the GDP-and GTP-bound forms of these proteins. Using Isothermal Titration Calorimetry, we have investigated interactions of IF2 and EF-G with the sarcin-ricin loop of the 23S rRNA, a crucial element of the GTPase-associated center of the ribosome. We show that binding of IF2 and EF-G to a 27 nucleotide RNA fragment mimicking the sarcin-ricin loop is mutually exclusive with that of GDP, but not of GTP, providing a mechanism for destabilization of the ribosome-bound GDP forms of translational GTPases.</p>}},
  author       = {{Mitkevich, Vladimir A. and Shyp, Viktoriya and Petrushanko, Irina Yu and Soosaar, Aksel and Atkinson, Gemma C. and Tenson, Tanel and Makarov, Alexander A. and Hauryliuk, Vasili}},
  issn         = {{2045-2322}},
  language     = {{eng}},
  pages        = {{1--6}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Scientific Reports}},
  title        = {{GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner}},
  url          = {{http://dx.doi.org/10.1038/srep00843}},
  doi          = {{10.1038/srep00843}},
  volume       = {{2}},
  year         = {{2012}},
}