Staying in the loop to make ends meet: roles and regulation of GlmR in .

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Main Authors: Suits, Logan, Khan, Sebastian J, Bhattacharya, Dipanwita, Dimitrova, Silviya, Eswara, Prahathees J
Format: Artículo científico
Language:en
Published: bioRxiv : the preprint server for biology 2025
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author Suits, Logan
Khan, Sebastian J
Bhattacharya, Dipanwita
Dimitrova, Silviya
Eswara, Prahathees J
author_facet Suits, Logan
Khan, Sebastian J
Bhattacharya, Dipanwita
Dimitrova, Silviya
Eswara, Prahathees J
Suits, Logan
Khan, Sebastian J
Bhattacharya, Dipanwita
Dimitrova, Silviya
Eswara, Prahathees J
collection PubMed - marine biology
contents Staying in the loop to make ends meet: roles and regulation of GlmR in . Suits, Logan Khan, Sebastian J Bhattacharya, Dipanwita Dimitrova, Silviya Eswara, Prahathees J The metabolic networks of most life forms integrate cost-benefit analysis to properly budget carbon and other essential nutrients through continuous assessment of nutrient availability and environmental threats. is a Gram-positive model bacterium found in diverse ecological niches such as soil, marine environments, and the human gut. As such, cells finetune metabolic pathways by monitoring signals indicating the presence of nutrients and stressors. A highly conserved protein, GlmR, is a key player in rationing carbon for the production of cell envelope precursors. This function of GlmR can be attributed to its role in cell shape regulation and antibiotic resistance. Given its central position in carbon utilization, GlmR is under post-translational regulation by phosphorylation and UDP-N-acetylglucosamine (UDP-GlcNAc) binding. GlmR is also linked to cyclic-di-AMP (c-di-AMP), a nucleotide second messenger involved in stress response. In this study, we probed the importance of GlmR in cell morphogenesis, c-di-AMP signaling, and investigated the physiological significance of post-translational regulation. Our results reveal that cells lacking exhibit: (i) increased susceptibility to tunicamycin, a cell envelope targeting antibiotic; (ii) impaired division site positioning; and (iii) elevated intracellular c-di-AMP concentration. Furthermore, we show that the function of GlmR is finetuned by UDP-GlcNAc binding, phosphorylation, and acetylation. Additionally, we provide evidence showing that the recently discovered enzymatic activity of GlmR is integral for its function. We show that GlmR is a cell width determinant and propose a model suggesting close cooperation with an actin-like protein, MreB. Overall, our studies highlight that GlmR is at the crux of carbon flux with an important role in maintaining cell envelope integrity.
format Artículo científico
id pubmed_41278741
institution PubMed
language en
publishDate 2025
publisher bioRxiv : the preprint server for biology
record_format pubmed
spellingShingle Staying in the loop to make ends meet: roles and regulation of GlmR in .
Suits, Logan
Khan, Sebastian J
Bhattacharya, Dipanwita
Dimitrova, Silviya
Eswara, Prahathees J
Staying in the loop to make ends meet: roles and regulation of GlmR in . Suits, Logan Khan, Sebastian J Bhattacharya, Dipanwita Dimitrova, Silviya Eswara, Prahathees J The metabolic networks of most life forms integrate cost-benefit analysis to properly budget carbon and other essential nutrients through continuous assessment of nutrient availability and environmental threats. is a Gram-positive model bacterium found in diverse ecological niches such as soil, marine environments, and the human gut. As such, cells finetune metabolic pathways by monitoring signals indicating the presence of nutrients and stressors. A highly conserved protein, GlmR, is a key player in rationing carbon for the production of cell envelope precursors. This function of GlmR can be attributed to its role in cell shape regulation and antibiotic resistance. Given its central position in carbon utilization, GlmR is under post-translational regulation by phosphorylation and UDP-N-acetylglucosamine (UDP-GlcNAc) binding. GlmR is also linked to cyclic-di-AMP (c-di-AMP), a nucleotide second messenger involved in stress response. In this study, we probed the importance of GlmR in cell morphogenesis, c-di-AMP signaling, and investigated the physiological significance of post-translational regulation. Our results reveal that cells lacking exhibit: (i) increased susceptibility to tunicamycin, a cell envelope targeting antibiotic; (ii) impaired division site positioning; and (iii) elevated intracellular c-di-AMP concentration. Furthermore, we show that the function of GlmR is finetuned by UDP-GlcNAc binding, phosphorylation, and acetylation. Additionally, we provide evidence showing that the recently discovered enzymatic activity of GlmR is integral for its function. We show that GlmR is a cell width determinant and propose a model suggesting close cooperation with an actin-like protein, MreB. Overall, our studies highlight that GlmR is at the crux of carbon flux with an important role in maintaining cell envelope integrity.
title Staying in the loop to make ends meet: roles and regulation of GlmR in .
url https://pubmed.ncbi.nlm.nih.gov/41278741/