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Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3

Hauryliuk, Vasili LU orcid ; Zavialov, Andrey ; Kisselev, Lev and Ehrenberg, Måns (2006) In Biochimie 88(7). p.747-757
Abstract

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 (KD(GDP) = 1.3 ± 0.2 μM, KD(GTP) ≈ 200 μM and KD(GDPNP) > 160 μM) as well as absence (KD(GDP) = 1.9 ± 0.3 μM, KD(GTP) 0.7 ± 0.2 μM and KD(GDPNP) ≈ 200 μM) of eRF1. From the present data we propose that (i) free eRF3 has a strong preference to bind GDP compared to GTP (ii) eRF3... (More)

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 (KD(GDP) = 1.3 ± 0.2 μM, KD(GTP) ≈ 200 μM and KD(GDPNP) > 160 μM) as well as absence (KD(GDP) = 1.9 ± 0.3 μM, KD(GTP) 0.7 ± 0.2 μM and KD(GDPNP) ≈ 200 μM) 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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author
; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
eRF1, eRF3, eukaryotes, GDPNP, GEF, GTPase, PABP, polypeptide release factors, translation termination
in
Biochimie
volume
88
issue
7
pages
11 pages
publisher
Elsevier
external identifiers
  • scopus:33746728252
  • pmid:16797113
ISSN
0300-9084
DOI
10.1016/j.biochi.2006.06.001
language
English
LU publication?
no
additional info
Funding Information: This work was supported by the Swedish Foundation for Strategic Research and the Swedish Research Council (M.E.), the Russian Academy of Sciences (program “Molecular and Cell Biology”), the Russian Foundation for Basic Research and the Program for Support of Leading Russian Scientific Schools via the Ministry of Education and Science (LK). Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
id
0f432179-16a4-4fc9-91cb-88163101e207
date added to LUP
2021-09-24 20:53:45
date last changed
2025-01-13 14:42:20
@article{0f432179-16a4-4fc9-91cb-88163101e207,
  abstract     = {{<p>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<sub>D</sub>(GDP) = 1.3 ± 0.2 μM, K<sub>D</sub>(GTP) ≈ 200 μM and K<sub>D</sub>(GDPNP) &gt; 160 μM) as well as absence (K<sub>D</sub>(GDP) = 1.9 ± 0.3 μM, K<sub>D</sub>(GTP) 0.7 ± 0.2 μM and K<sub>D</sub>(GDPNP) ≈ 200 μM) 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.</p>}},
  author       = {{Hauryliuk, Vasili and Zavialov, Andrey and Kisselev, Lev and Ehrenberg, Måns}},
  issn         = {{0300-9084}},
  keywords     = {{eRF1; eRF3; eukaryotes; GDPNP; GEF; GTPase; PABP; polypeptide release factors; translation termination}},
  language     = {{eng}},
  number       = {{7}},
  pages        = {{747--757}},
  publisher    = {{Elsevier}},
  series       = {{Biochimie}},
  title        = {{Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3}},
  url          = {{http://dx.doi.org/10.1016/j.biochi.2006.06.001}},
  doi          = {{10.1016/j.biochi.2006.06.001}},
  volume       = {{88}},
  year         = {{2006}},
}