Open Access
FEBS Journal, volume 277, issue 12, pages 2611-2627
NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor
Ivanova Elena V
2, 3, 4
,
Birdsall Berry
5
,
Алкалаева Е. З.
2, 3, 4
,
Kryuchkova Polina N
6, 7
,
Kelly Geoff
8
,
Frolova Ludmila Y
2, 3, 4
,
1
3
RUSSIAN ACADEMY OF SCIENCES
4
Moscow Russia
|
5
Division of Molecular Structure, MRC-National Institute for Medical Research, London, UK
|
8
MRC Biomedical NMR Centre, NIMR, London, UK
|
Publication type: Journal Article
Publication date: 2010-05-11
Journal:
FEBS Journal
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 5.4
ISSN: 1742464X, 14321033
PubMed ID:
20553496
Biochemistry
Molecular Biology
Cell Biology
Abstract
Termination of translation in eukaryotes is triggered by two polypeptide chain release factors, eukaryotic class 1 polypeptide chain release factor (eRF1) and eukaryotic class 2 polypeptide chain release factor 3. eRF1 is a three‐domain protein that interacts with eukaryotic class 2 polypeptide chain release factor 3 via its C‐terminal domain (C‐domain). The high‐resolution NMR structure of the human C‐domain (residues 277–437) has been determined in solution. The overall fold and the structure of the β‐strand core of the protein in solution are similar to those found in the crystal structure. The structure of the minidomain (residues 329–372), which was ill‐defined in the crystal structure, has been determined in solution. The protein backbone dynamics, studied using 15N‐relaxation experiments, showed that the C‐terminal tail 414–437 and the minidomain are the most flexible parts of the human C‐domain. The minidomain exists in solution in two conformational states, slowly interconverting on the NMR timescale. Superposition of this NMR solution structure of the human C‐domain onto the available crystal structure of full‐length human eRF1 shows that the minidomain is close to the stop codon‐recognizing N‐terminal domain. Mutations in the tip of the minidomain were found to affect the stop codon specificity of the factor. The results provide new insights into the possible role of the C‐domain in the process of translation termination.
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- We do not take into account publications that without a DOI.
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- Statistics recalculated weekly.
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Mantsyzov A. B. et al. NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor // FEBS Journal. 2010. Vol. 277. No. 12. pp. 2611-2627.
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Mantsyzov A. B., Ivanova E. V., Birdsall B., Алкалаева Е. З., Kryuchkova P. N., Kelly G., Frolova L. Y., Polshakov V. I. NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor // FEBS Journal. 2010. Vol. 277. No. 12. pp. 2611-2627.
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TY - JOUR
DO - 10.1111/j.1742-4658.2010.07672.x
UR - https://doi.org/10.1111%2Fj.1742-4658.2010.07672.x
TI - NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor
T2 - FEBS Journal
AU - Mantsyzov, Alexey B.
AU - Ivanova, Elena V
AU - Birdsall, Berry
AU - Kryuchkova, Polina N
AU - Frolova, Ludmila Y
AU - Алкалаева, Е. З.
AU - Kelly, Geoff
AU - Polshakov, Vladimir I.
PY - 2010
DA - 2010/05/11 00:00:00
PB - Wiley
SP - 2611-2627
IS - 12
VL - 277
PMID - 20553496
SN - 1742-464X
SN - 1432-1033
ER -
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@article{2010_Mantsyzov,
author = {Alexey B. Mantsyzov and Elena V Ivanova and Berry Birdsall and Polina N Kryuchkova and Ludmila Y Frolova and Е. З. Алкалаева and Geoff Kelly and Vladimir I. Polshakov},
title = {NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor},
journal = {FEBS Journal},
year = {2010},
volume = {277},
publisher = {Wiley},
month = {may},
url = {https://doi.org/10.1111%2Fj.1742-4658.2010.07672.x},
number = {12},
pages = {2611--2627},
doi = {10.1111/j.1742-4658.2010.07672.x}
}
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Mantsyzov, Alexey B., et al. “NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor.” FEBS Journal, vol. 277, no. 12, May. 2010, pp. 2611-2627. https://doi.org/10.1111%2Fj.1742-4658.2010.07672.x.
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