Open Access
Nucleic Acids Research, volume 44, issue 12, pages 5798-5810
The extended loops of ribosomal proteins uL4 and uL22 ofEscherichia colicontribute to ribosome assembly and protein translation
Lawrence Marlon G
1
,
Shamsuzzaman Md
1
,
Kondopaka Maithri
1
,
Pascual Clarence
1
,
Zengel Janice M.
1
,
Lindahl Lasse
1
1
Department of Biological Sciences, University of Maryland, Baltimore County, Baltimore, MD, 21250, USA
|
Publication type: Journal Article
Publication date: 2016-06-01
Journal:
Nucleic Acids Research
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 14.9
ISSN: 03051048, 13624962
PubMed ID:
27257065
Genetics
Abstract
Nearly half of ribosomal proteins are composed of a domain on the ribosome surface and a loop or extension that penetrates into the organelle's RNA core. Our previous work showed that ribosomes lacking the loops of ribosomal proteins uL4 or uL22 are still capable of entering polysomes. However, in those experiments we could not address the formation of mutant ribosomes, because we used strains that also expressed wild-type uL4 and uL22. Here, we have focused on ribosome assembly and function in strains in which loop deletion mutant genes are the only sources of uL4 or uL22 protein. The uL4 and uL22 loop deletions have different effects, but both mutations result in accumulation of immature particles that do not accumulate in detectable amounts in wild-type strains. Thus, our results suggest that deleting the loops creates kinetic barriers in the normal assembly pathway, possibly resulting in assembly via alternate pathway(s). Furthermore, deletion of the uL4 loop results in cold-sensitive ribosome assembly and function. Finally, ribosomes carrying either of the loop-deleted proteins responded normally to the secM translation pausing peptide, but the uL4 mutant responded very inefficiently to the cmlAcrb pause peptide.
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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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Lawrence M. G. et al. The extended loops of ribosomal proteins uL4 and uL22 ofEscherichia colicontribute to ribosome assembly and protein translation // Nucleic Acids Research. 2016. Vol. 44. No. 12. pp. 5798-5810.
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Lawrence M. G., Shamsuzzaman M., Kondopaka M., Pascual C., Zengel J. M., Lindahl L. The extended loops of ribosomal proteins uL4 and uL22 ofEscherichia colicontribute to ribosome assembly and protein translation // Nucleic Acids Research. 2016. Vol. 44. No. 12. pp. 5798-5810.
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TY - JOUR
DO - 10.1093/nar/gkw493
UR - https://doi.org/10.1093%2Fnar%2Fgkw493
TI - The extended loops of ribosomal proteins uL4 and uL22 ofEscherichia colicontribute to ribosome assembly and protein translation
T2 - Nucleic Acids Research
AU - Lawrence, Marlon G
AU - Shamsuzzaman, Md
AU - Kondopaka, Maithri
AU - Pascual, Clarence
AU - Zengel, Janice M.
AU - Lindahl, Lasse
PY - 2016
DA - 2016/06/01 00:00:00
PB - Oxford University Press
SP - 5798-5810
IS - 12
VL - 44
PMID - 27257065
SN - 0305-1048
SN - 1362-4962
ER -
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@article{2016_Lawrence,
author = {Marlon G Lawrence and Md Shamsuzzaman and Maithri Kondopaka and Clarence Pascual and Janice M. Zengel and Lasse Lindahl},
title = {The extended loops of ribosomal proteins uL4 and uL22 ofEscherichia colicontribute to ribosome assembly and protein translation},
journal = {Nucleic Acids Research},
year = {2016},
volume = {44},
publisher = {Oxford University Press},
month = {jun},
url = {https://doi.org/10.1093%2Fnar%2Fgkw493},
number = {12},
pages = {5798--5810},
doi = {10.1093/nar/gkw493}
}
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Lawrence, Marlon G., et al. “The extended loops of ribosomal proteins uL4 and uL22 ofEscherichia colicontribute to ribosome assembly and protein translation.” Nucleic Acids Research, vol. 44, no. 12, Jun. 2016, pp. 5798-5810. https://doi.org/10.1093%2Fnar%2Fgkw493.