GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner
(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.
(Less)
- author
- Mitkevich, Vladimir A. ; Shyp, Viktoriya ; Petrushanko, Irina Yu ; Soosaar, Aksel ; Atkinson, Gemma C. LU ; Tenson, Tanel ; Makarov, Alexander A. and Hauryliuk, Vasili LU
- publishing date
- 2012
- 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}}, }