Biochemistry, volume 47, issue 34, pages 8828-8839
Conservation of Bacterial Protein Synthesis Machinery: Initiation and Elongation in Mycobacterium smegmatis
Bruell Christian M
1
,
Eichholz Carolin
1
,
Kubarenko Andriy
1
,
Post Virginia
1
,
Katunin Vladimir I.
1
,
Hobbie Sven N
1
,
Rodnina Marina V.
1
,
Böttger Erik C.
1
Publication type: Journal Article
Publication date: 2008-08-01
Journal:
Biochemistry
Quartile SCImago
Q1
Quartile WOS
Q3
Impact factor: 2.9
ISSN: 00062960, 15204995
Biochemistry
Abstract
Most of our understanding of ribosome function is based on experiments utilizing translational components from Escherichia coli. It is not clear to which extent the details of translation mechanisms derived from this single organism are true for all bacteria. Here we investigate translation factor-dependent reactions of initiation and elongation in a reconstituted translation system from a Gram-positive bacterium Mycobacterium smegmatis. This organism was chosen because mutations in rRNA have very different phenotypes in E. coli and M. smegmatis, and the docking site for translational GTPases, the L12 stalk, is extended in the ribosomes from M. smegmatis compared to E. coli. M. smegmatis genes coding for IF1, IF2, IF3, EF-G, and EF-Tu were identified by sequence alignments; the respective recombinant proteins were prepared and studied in a variety of biochemical and biophysical assays with M. smegmatis ribosomes. We found that the activities of initiation and elongation factors and the rates of elemental reactions of initiation and elongation of protein synthesis are remarkably similar with M. smegmatis and E. coli components. The data suggest a very high degree of conservation of basic translation mechanisms, probably due to coevolution of the ribosome components and translation factors. This work establishes the reconstituted translation system from individual purified M. smegmatis components as an alternative to that from E. coli to study the mechanisms of translation and to test the action of antibiotics against Gram-positive bacteria.
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Citations by publishers
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1 publication, 4.76%
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1 publication, 4.76%
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Bruell C. M. et al. Conservation of Bacterial Protein Synthesis Machinery: Initiation and Elongation in Mycobacterium smegmatis // Biochemistry. 2008. Vol. 47. No. 34. pp. 8828-8839.
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Bruell C. M., Eichholz C., Kubarenko A., Post V., Katunin V. I., Hobbie S. N., Rodnina M. V., Böttger E. C. Conservation of Bacterial Protein Synthesis Machinery: Initiation and Elongation in Mycobacterium smegmatis // Biochemistry. 2008. Vol. 47. No. 34. pp. 8828-8839.
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TY - JOUR
DO - 10.1021/bi800527k
UR - https://doi.org/10.1021%2Fbi800527k
TI - Conservation of Bacterial Protein Synthesis Machinery: Initiation and Elongation in Mycobacterium smegmatis
T2 - Biochemistry
AU - Bruell, Christian M
AU - Eichholz, Carolin
AU - Kubarenko, Andriy
AU - Post, Virginia
AU - Katunin, Vladimir I.
AU - Hobbie, Sven N
AU - Böttger, Erik C.
AU - Rodnina, Marina V.
PY - 2008
DA - 2008/08/01 00:00:00
PB - American Chemical Society (ACS)
SP - 8828-8839
IS - 34
VL - 47
SN - 0006-2960
SN - 1520-4995
ER -
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@article{2008_Bruell,
author = {Christian M Bruell and Carolin Eichholz and Andriy Kubarenko and Virginia Post and Vladimir I. Katunin and Sven N Hobbie and Erik C. Böttger and Marina V. Rodnina},
title = {Conservation of Bacterial Protein Synthesis Machinery: Initiation and Elongation in Mycobacterium smegmatis},
journal = {Biochemistry},
year = {2008},
volume = {47},
publisher = {American Chemical Society (ACS)},
month = {aug},
url = {https://doi.org/10.1021%2Fbi800527k},
number = {34},
pages = {8828--8839},
doi = {10.1021/bi800527k}
}
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MLA
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Bruell, Christian M., et al. “Conservation of Bacterial Protein Synthesis Machinery: Initiation and Elongation in Mycobacterium smegmatis.” Biochemistry, vol. 47, no. 34, Aug. 2008, pp. 8828-8839. https://doi.org/10.1021%2Fbi800527k.