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Activation of initiation factor 2 by ligands and mutations for rapid docking of ribosomal subunits
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
2011 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 30, no 2, 289-301 p.Article in journal (Refereed) Published
Abstract [en]

We previously identified mutations in the GTPase initiation factor 2 (IF2), located outside its tRNA-binding domain, compensating strongly (A-type) or weakly (B-type) for initiator tRNA formylation deficiency. We show here that rapid docking of 30S with 50S subunits in initiation of translation depends on switching 30S subunit-bound IF2 from its inactive to active form. Activation of wild-type IF2 requires GTP and formylated initiator tRNA (fMet-tRNA(i)). In contrast, extensive activation of A-type IF2 occurs with only GTP or with GDP and fMet-tRNA(i), implying a passive role for initiator tRNA as activator of IF2 in subunit docking. The theory of conditional switching of GTPases quantitatively accounts for all our experimental data. We find that GTP, GDP, fMet-tRNA(i) and A-type mutations multiplicatively increase the equilibrium ratio, K, between active and inactive forms of IF2 from a value of 4 × 10(-4) for wild-type apo-IF2 by factors of 300, 8, 80 and 20, respectively. Functional characterization of the A-type mutations provides keys to structural interpretation of conditional switching of IF2 and other multidomain GTPases.

 

Place, publisher, year, edition, pages
2011. Vol. 30, no 2, 289-301 p.
Keyword [en]
conformational switching, GTPAses, initiation factors, initiator tRNA, protein synthesis
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-145814DOI: 10.1038/emboj.2010.328ISI: 000287179100007PubMedID: 21151095OAI: oai:DiVA.org:uu-145814DiVA: diva2:396923
Available from: 2011-02-11 Created: 2011-02-11 Last updated: 2017-12-11Bibliographically approved

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Andersson, Dan I.

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