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Journal of Biological Chemistry, volume 280, issue 36, pages 31882-31889

Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G

Lesnyak Dmitry V 2
Burakovsky Dmitry E 1
Kiparisov Sergey V 1
Leonov Andrei A. 1
Bogdanov Alexey A. 1
BRIMACOMBE RICHARD 3
Publication typeJournal Article
Publication date2005-09-01
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor4.8
ISSN00219258, 1083351X
Biochemistry
Molecular Biology
Cell Biology
Abstract
Translocation catalyzed by elongation factor G occurs after the peptidyltransferase reaction on the large ribosomal subunit. Deacylated tRNA in the P-site stimulates multiple turnover GTPase activity of EF-G. We suggest that the allosteric signal from the peptidyltransferase center that activates EF-G may involve the alteration in the conformation of elongation factor binding center of the ribosome. The latter consists of the moveable GTPase-associated center and the sarcin-ricin loop that keeps its position on the ribosome during translation elongation. The position of the GTPase-associated center was altered by mutagenesis. An insertion of additional base pair at positions C1030/G1124 was lethal and affected function of EF-G, but not that of EF-Tu. Structure probing revealed a putative allosteric signal pathway connecting the P-site with the binding site of the elongation factors. The results are consistent with the different structural requirements for EF-G and EF-Tu function, where the integrity of the path between the peptidyltransferase center and both GTPase-associated center and sarcin-ricin loop is important for EF-G binding.

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GOST Copy
Sergiev P. V. et al. Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G // Journal of Biological Chemistry. 2005. Vol. 280. No. 36. pp. 31882-31889.
GOST all authors (up to 50) Copy
Sergiev P. V., Lesnyak D. V., Burakovsky D. E., Kiparisov S. V., Leonov A. A., Bogdanov A. A., BRIMACOMBE R., Dontsova O. A. Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G // Journal of Biological Chemistry. 2005. Vol. 280. No. 36. pp. 31882-31889.
RIS |
Cite this
RIS Copy
TY - JOUR
DO - 10.1074/jbc.M505670200
UR - https://doi.org/10.1074%2Fjbc.M505670200
TI - Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G
T2 - Journal of Biological Chemistry
AU - Sergiev, Petr V.
AU - Lesnyak, Dmitry V
AU - Burakovsky, Dmitry E
AU - Kiparisov, Sergey V
AU - Leonov, Andrei A.
AU - Bogdanov, Alexey A.
AU - BRIMACOMBE, RICHARD
AU - Dontsova, Olga A.
PY - 2005
DA - 2005/09/01 00:00:00
PB - American Society for Biochemistry and Molecular Biology
SP - 31882-31889
IS - 36
VL - 280
SN - 0021-9258
SN - 1083-351X
ER -
BibTex |
Cite this
BibTex Copy
@article{2005_Sergiev,
author = {Petr V. Sergiev and Dmitry V Lesnyak and Dmitry E Burakovsky and Sergey V Kiparisov and Andrei A. Leonov and Alexey A. Bogdanov and RICHARD BRIMACOMBE and Olga A. Dontsova},
title = {Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G},
journal = {Journal of Biological Chemistry},
year = {2005},
volume = {280},
publisher = {American Society for Biochemistry and Molecular Biology},
month = {sep},
url = {https://doi.org/10.1074%2Fjbc.M505670200},
number = {36},
pages = {31882--31889},
doi = {10.1074/jbc.M505670200}
}
MLA
Cite this
MLA Copy
Sergiev, Petr V., et al. “Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G.” Journal of Biological Chemistry, vol. 280, no. 36, Sep. 2005, pp. 31882-31889. https://doi.org/10.1074%2Fjbc.M505670200.
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