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Escherichia coli ut...
Escherichia coli utilizes multiple peptidoglycan recycling permeases with distinct strategies of recycling
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- Simpson, Brent W. (author)
- Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, United States
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- Gilmore, Michael C. (author)
- Umeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)
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- McLean, Amanda Briann (author)
- Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, United States
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- Cava, Felipe (author)
- Umeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)
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- Trent, M. Stephen (author)
- Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, United States; Department of Microbiology, College of Art and Sciences, University of Georgia, Athens, United States
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(creator_code:org_t)
- Proceedings of the National Academy of Sciences (PNAS), 2023
- 2023
- English.
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In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences (PNAS). - 0027-8424 .- 1091-6490. ; 120:44
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https://umu.diva-por... (primary) (Raw object)
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Abstract
Subject headings
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- Bacteria produce a structural layer of peptidoglycan (PG) that enforces cell shape, resists turgor pressure, and protects the cell. As bacteria grow and divide, the existing layer of PG is remodeled and PG fragments are released. Enterics such as Escherichia coli go to great lengths to internalize and reutilize PG fragments. E. coli is estimated to break down one-third of its cell wall, yet only loses ~0 to 5% of meso-diaminopimelic acid, a PG-specific amino acid, per generation. Two transporters were identified early on to possibly be the primary permease that facilitates PG fragment recycling, i) AmpG and ii) the Opp ATP binding cassette transporter in conjunction with a PG-specific periplasmic binding protein, MppA. The contribution of each transporter to PG recycling has been debated. Here, we have found that AmpG and MppA/Opp are differentially regulated by carbon source and growth phase. In addition, MppA/Opp is uniquely capable of high-affinity scavenging of muropeptides from growth media, demonstrating that AmpG and MppA/Opp allow for different strategies of recycling PG fragments. Altogether, this work clarifies environmental contexts under which E. coli utilizes distinct permeases for PG recycling and explores how scavenging by MppA/Opp could be beneficial in mixed communities.
Subject headings
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
Keyword
- AmpG
- cell wall
- muropeptides
- peptidoglycan
- peptidoglycan recycling
Publication and Content Type
- ref (subject category)
- art (subject category)
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