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  • 1. Andreev, Dmitri
    et al.
    Hauryliuk, Vasili
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Terenin, Ilya
    Dmitriev, Sergey
    Ehrenberg, Måns
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Shatsky, Ivan
    The bacterial toxin ReIE induces specific mRNA cleavage in the A site of the eukaryote ribosome2008In: RNA: A publication of the RNA Society, ISSN 1355-8382, E-ISSN 1469-9001, Vol. 14, no 2, p. 233-239Article in journal (Refereed)
    Abstract [en]

    ReIE/ReIB is a well-characterized toxin-anti-toxin pair involved in nutritional stress responses in Bacteria and Archae. ReIE lacks any eukaryote homolog, but we demonstrate here that it efficiently and specifically cleaves mRNA in the A site of the eukaryote ribosome. The cleavage mechanism is similar to that in bacteria, showing the feasibility of A-site cleavage of mRNA for regulatory purposes also in eukaryotes. ReIE cleavage in the A-site codon of a stalled eukaryote ribosome is precise and easily monitored, making "ReIE printing" a useful complement to toeprinting to determine the exact mRNA location on the eukaryote ribosome and to probe the occupancy of its A site.

  • 2.
    Ehrenberg, Måns
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Biology.
    Hauryliuk, Vasili
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Biology.
    Crist, Colin G
    Nakamura, Yoshikazu
    Translation Termination, the Prion [Psi+], and Ribosomal Recycling2007In: Translational Control in Biology and Medicine / [ed] Michael B. Mathews, Nahum Sonenberg & John W.B. Hershey, Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press , 2007, p. 173-196Chapter in book (Other academic)
  • 3.
    Hauryliuk, Vasili
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Molekylärbiologi.
    Ehrenberg, Måns
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Molekylärbiologi.
    Two-step selection of mRNAs in initiation of protein synthesis.2006In: Mol Cell, ISSN 1097-2765, Vol. 22, no 2, p. 155-6Article in journal (Refereed)
  • 4.
    Hauryliuk, Vasili
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Zavialov, Andrey
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Kisselev, Lev
    Ehrenberg, Måns
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF32006In: Biochimie, ISSN 0300-9084, E-ISSN 1638-6183, Vol. 88, no 7, p. 747-757Article in journal (Refereed)
    Abstract [en]

    In eukaryotes, termination of mRNA translation is triggered by the essential polypeptide chain release factors eRF1, recognizing all three stop codons, and eRF3, a member of the GTPase superfamily with a role that has remained opaque. We have studied the kinetic and thermodynamic parameters of the interactions between eRF3 and GTP, GDP and the non-hydrolysable GTP analogue GDPNP in the presence (K-D(GDP) = 1.3 +/- 0.2 mu M, K-D(GTP) approximate to 200 mu M and K-D(GDPNP) > 160 mu M) as well as absence (K-D(GDP) = 1.9 +/- 0.3 mu M, K-D(GTP) 0.7 +/- 0.2 mu M and K-D(GDPNP) approximate to 200 mu M) of eRF1. From the present data we propose that (i) free eRF3 has a strong preference to bind GDP compared to GTP (ii) eRF3 in complex with eRF1 has much stronger affinity to GTP than free eRF3 (iii) eRF3 in complex with PABP has weak affinity to GTP (iv) eRF3 in complex with eRF1 does not have strong affinity to GDPNP, implying that GDPNP is a poor analogue of GTP for eRF3 binding.

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