ActS activates peptidoglycan amidases during outer membrane stress in Escherichia coli. Issue 1 (23rd March 2021)
- Record Type:
- Journal Article
- Title:
- ActS activates peptidoglycan amidases during outer membrane stress in Escherichia coli. Issue 1 (23rd March 2021)
- Main Title:
- ActS activates peptidoglycan amidases during outer membrane stress in Escherichia coli
- Authors:
- Gurnani Serrano, Carlos K.
Winkle, Matthias
Martorana, Alessandra M.
Biboy, Jacob
Morè, Niccolo
Moynihan, Patrick
Banzhaf, Manuel
Vollmer, Waldemar
Polissi, Alessandra - Abstract:
- Abstract: The integrity of the cell envelope of E. coli relies on the concerted activity of multi‐protein machineries that synthesize the peptidoglycan (PG) and the outer membrane (OM). Our previous work found that the depletion of lipopolysaccharide (LPS) export to the OM induces an essential PG remodeling process involving LD‐transpeptidases (LDTs), the glycosyltransferase function of PBP1B and the carboxypeptidase PBP6a. Consequently, cells with defective OM biogenesis lyse if they lack any of these PG enzymes. Here we report that the morphological defects, and lysis associated with a ldtF mutant with impaired LPS transport, are alleviated by the loss of the predicted OM‐anchored lipoprotein ActS (formerly YgeR). We show that ActS is an inactive member of LytM‐type peptidoglycan endopeptidases due to a degenerated catalytic domain. ActS is capable of activating all three main periplasmic peptidoglycan amidases, AmiA, AmiB, and AmiC, which were previously reported to be activated only by EnvC and/or NlpD. Our data also suggest that in vivo ActS preferentially activates AmiC and that its function is linked to cell envelope stress. Abstract : ActS activity in stressed cells is somehow controlled by LdtF resulting in mild chaining phenotype (left panel). Deletion of ldtF leads to spurious ActS activation causing cell lysis (central panel). Deletion of actS in cells lacking LdtF suppresses the lysis phenotype (right panel). At this condition AmiC is sufficiently controlled byAbstract: The integrity of the cell envelope of E. coli relies on the concerted activity of multi‐protein machineries that synthesize the peptidoglycan (PG) and the outer membrane (OM). Our previous work found that the depletion of lipopolysaccharide (LPS) export to the OM induces an essential PG remodeling process involving LD‐transpeptidases (LDTs), the glycosyltransferase function of PBP1B and the carboxypeptidase PBP6a. Consequently, cells with defective OM biogenesis lyse if they lack any of these PG enzymes. Here we report that the morphological defects, and lysis associated with a ldtF mutant with impaired LPS transport, are alleviated by the loss of the predicted OM‐anchored lipoprotein ActS (formerly YgeR). We show that ActS is an inactive member of LytM‐type peptidoglycan endopeptidases due to a degenerated catalytic domain. ActS is capable of activating all three main periplasmic peptidoglycan amidases, AmiA, AmiB, and AmiC, which were previously reported to be activated only by EnvC and/or NlpD. Our data also suggest that in vivo ActS preferentially activates AmiC and that its function is linked to cell envelope stress. Abstract : ActS activity in stressed cells is somehow controlled by LdtF resulting in mild chaining phenotype (left panel). Deletion of ldtF leads to spurious ActS activation causing cell lysis (central panel). Deletion of actS in cells lacking LdtF suppresses the lysis phenotype (right panel). At this condition AmiC is sufficiently controlled by NlpD enabling it to partially restore cell separation. … (more)
- Is Part Of:
- Molecular microbiology. Volume 116:Issue 1(2021)
- Journal:
- Molecular microbiology
- Issue:
- Volume 116:Issue 1(2021)
- Issue Display:
- Volume 116, Issue 1 (2021)
- Year:
- 2021
- Volume:
- 116
- Issue:
- 1
- Issue Sort Value:
- 2021-0116-0001-0000
- Page Start:
- 329
- Page End:
- 342
- Publication Date:
- 2021-03-23
- Subjects:
- cell division -- cell envelope -- Escherichia coli -- lipopolysaccharide -- peptidoglycan
Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.14712 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 17566.xml