Cargando…
Regulation of Translation by Lysine Acetylation in Escherichia coli
Nε-lysine acetylation is a common posttranslational modification observed in diverse species of bacteria. Aside from a few central metabolic enzymes and transcription factors, little is known about how this posttranslational modification regulates protein activity. In this work, we investigated how...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Microbiology
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9239087/ https://www.ncbi.nlm.nih.gov/pubmed/35604121 http://dx.doi.org/10.1128/mbio.01224-22 |
_version_ | 1784737211932999680 |
---|---|
author | Feid, Sarah C. Walukiewicz, Hanna E. Wang, Xiaoyi Nakayasu, Ernesto S. Rao, Christopher V. Wolfe, Alan J. |
author_facet | Feid, Sarah C. Walukiewicz, Hanna E. Wang, Xiaoyi Nakayasu, Ernesto S. Rao, Christopher V. Wolfe, Alan J. |
author_sort | Feid, Sarah C. |
collection | PubMed |
description | Nε-lysine acetylation is a common posttranslational modification observed in diverse species of bacteria. Aside from a few central metabolic enzymes and transcription factors, little is known about how this posttranslational modification regulates protein activity. In this work, we investigated how lysine acetylation affects translation in Escherichia coli. In multiple species of bacteria, ribosomal proteins are highly acetylated at conserved lysine residues, suggesting that this modification may regulate translation. In support of this hypothesis, we found that the addition of either of the acetyl donors acetyl phosphate and acetyl-coenzyme A inhibits translation but not transcription using an E. coli cell-free system. Further investigations using in vivo assays revealed that acetylation does not appear to alter the rate of translation elongation but, rather, increases the proportions of dissociated 30S and 50S ribosomes, based on polysome profiles of mutants or growth conditions known to promote lysine acetylation. Furthermore, ribosomal proteins are more acetylated in the disassociated 30S and 50S ribosomal subunits than in the fully assembled 70S complex. The effect of acetylation is also growth rate dependent, with disassociation of the subunits being most pronounced during late-exponential and early-stationary-phase growth—the same growth phase where protein acetylation is greatest. Collectively, our data demonstrate that lysine acetylation inhibits translation, most likely by interfering with subunit association. These results have also uncovered a new mechanism for coupling translation to the metabolic state of the cell. |
format | Online Article Text |
id | pubmed-9239087 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Society for Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-92390872022-06-29 Regulation of Translation by Lysine Acetylation in Escherichia coli Feid, Sarah C. Walukiewicz, Hanna E. Wang, Xiaoyi Nakayasu, Ernesto S. Rao, Christopher V. Wolfe, Alan J. mBio Research Article Nε-lysine acetylation is a common posttranslational modification observed in diverse species of bacteria. Aside from a few central metabolic enzymes and transcription factors, little is known about how this posttranslational modification regulates protein activity. In this work, we investigated how lysine acetylation affects translation in Escherichia coli. In multiple species of bacteria, ribosomal proteins are highly acetylated at conserved lysine residues, suggesting that this modification may regulate translation. In support of this hypothesis, we found that the addition of either of the acetyl donors acetyl phosphate and acetyl-coenzyme A inhibits translation but not transcription using an E. coli cell-free system. Further investigations using in vivo assays revealed that acetylation does not appear to alter the rate of translation elongation but, rather, increases the proportions of dissociated 30S and 50S ribosomes, based on polysome profiles of mutants or growth conditions known to promote lysine acetylation. Furthermore, ribosomal proteins are more acetylated in the disassociated 30S and 50S ribosomal subunits than in the fully assembled 70S complex. The effect of acetylation is also growth rate dependent, with disassociation of the subunits being most pronounced during late-exponential and early-stationary-phase growth—the same growth phase where protein acetylation is greatest. Collectively, our data demonstrate that lysine acetylation inhibits translation, most likely by interfering with subunit association. These results have also uncovered a new mechanism for coupling translation to the metabolic state of the cell. American Society for Microbiology 2022-05-23 /pmc/articles/PMC9239087/ /pubmed/35604121 http://dx.doi.org/10.1128/mbio.01224-22 Text en Copyright © 2022 Feid et al. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Research Article Feid, Sarah C. Walukiewicz, Hanna E. Wang, Xiaoyi Nakayasu, Ernesto S. Rao, Christopher V. Wolfe, Alan J. Regulation of Translation by Lysine Acetylation in Escherichia coli |
title | Regulation of Translation by Lysine Acetylation in Escherichia coli |
title_full | Regulation of Translation by Lysine Acetylation in Escherichia coli |
title_fullStr | Regulation of Translation by Lysine Acetylation in Escherichia coli |
title_full_unstemmed | Regulation of Translation by Lysine Acetylation in Escherichia coli |
title_short | Regulation of Translation by Lysine Acetylation in Escherichia coli |
title_sort | regulation of translation by lysine acetylation in escherichia coli |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9239087/ https://www.ncbi.nlm.nih.gov/pubmed/35604121 http://dx.doi.org/10.1128/mbio.01224-22 |
work_keys_str_mv | AT feidsarahc regulationoftranslationbylysineacetylationinescherichiacoli AT walukiewiczhannae regulationoftranslationbylysineacetylationinescherichiacoli AT wangxiaoyi regulationoftranslationbylysineacetylationinescherichiacoli AT nakayasuernestos regulationoftranslationbylysineacetylationinescherichiacoli AT raochristopherv regulationoftranslationbylysineacetylationinescherichiacoli AT wolfealanj regulationoftranslationbylysineacetylationinescherichiacoli |