Unusual 1-3 peptidoglycan cross-links in Acetobacteraceae are made by L,D-transpeptidases with a catalytic domain distantly related to YkuD domains
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved..
Peptidoglycan is an essential component of the bacterial cell envelope that contains glycan chains substituted by short peptide stems. Peptide stems are polymerized by D,D-transpeptidases, which make bonds between the amino acid in position four of a donor stem and the third residue of an acceptor stem (4-3 cross-links). Some bacterial peptidoglycans also contain 3-3 cross-links that are formed by another class of enzymes called L,D-transpeptidases which contain a YkuD catalytic domain. In this work, we investigate the formation of unusual bacterial 1-3 peptidoglycan cross-links. We describe a version of the PGFinder software that can identify 1-3 cross-links and report the high-resolution peptidoglycan structure of Gluconobacter oxydans (a model organism within the Acetobacteraceae family). We reveal that G. oxydans peptidoglycan contains peptide stems made of a single alanine as well as several dipeptide stems with unusual amino acids at their C-terminus. Using a bioinformatics approach, we identified a G. oxydans mutant from a transposon library with a drastic reduction in 1-3 cross-links. Through complementation experiments in G. oxydans and recombinant protein production in a heterologous host, we identify an L,D-transpeptidase enzyme with a domain distantly related to the YkuD domain responsible for these non-canonical reactions. This work revisits the enzymatic capabilities of L,D-transpeptidases, a versatile family of enzymes that play a key role in bacterial peptidoglycan remodelling.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:300 |
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| Enthalten in: |
The Journal of biological chemistry - 300(2024), 1 vom: 11. Jan., Seite 105494 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Alamán-Zárate, Marcel G [VerfasserIn] |
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| Links: |
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| Themen: |
Amino Acids |
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| Anmerkungen: |
Date Completed 08.02.2024 Date Revised 13.03.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.jbc.2023.105494 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM364981644 |
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| 100 | 1 | |a Alamán-Zárate, Marcel G |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Unusual 1-3 peptidoglycan cross-links in Acetobacteraceae are made by L,D-transpeptidases with a catalytic domain distantly related to YkuD domains |
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| 520 | |a Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved. | ||
| 520 | |a Peptidoglycan is an essential component of the bacterial cell envelope that contains glycan chains substituted by short peptide stems. Peptide stems are polymerized by D,D-transpeptidases, which make bonds between the amino acid in position four of a donor stem and the third residue of an acceptor stem (4-3 cross-links). Some bacterial peptidoglycans also contain 3-3 cross-links that are formed by another class of enzymes called L,D-transpeptidases which contain a YkuD catalytic domain. In this work, we investigate the formation of unusual bacterial 1-3 peptidoglycan cross-links. We describe a version of the PGFinder software that can identify 1-3 cross-links and report the high-resolution peptidoglycan structure of Gluconobacter oxydans (a model organism within the Acetobacteraceae family). We reveal that G. oxydans peptidoglycan contains peptide stems made of a single alanine as well as several dipeptide stems with unusual amino acids at their C-terminus. Using a bioinformatics approach, we identified a G. oxydans mutant from a transposon library with a drastic reduction in 1-3 cross-links. Through complementation experiments in G. oxydans and recombinant protein production in a heterologous host, we identify an L,D-transpeptidase enzyme with a domain distantly related to the YkuD domain responsible for these non-canonical reactions. This work revisits the enzymatic capabilities of L,D-transpeptidases, a versatile family of enzymes that play a key role in bacterial peptidoglycan remodelling | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Gluconobacter oxydans | |
| 650 | 4 | |a L,D-transpeptidase | |
| 650 | 4 | |a PGFinder | |
| 650 | 4 | |a bacterial cell envelope | |
| 650 | 4 | |a crosslink | |
| 650 | 4 | |a peptidoglycan | |
| 650 | 7 | |a Amino Acids |2 NLM | |
| 650 | 7 | |a Bacterial Proteins |2 NLM | |
| 650 | 7 | |a Peptidoglycan |2 NLM | |
| 650 | 7 | |a Peptidyl Transferases |2 NLM | |
| 650 | 7 | |a EC 2.3.2.12 |2 NLM | |
| 700 | 1 | |a Rady, Brooks J |e verfasserin |4 aut | |
| 700 | 1 | |a Evans, Caroline A |e verfasserin |4 aut | |
| 700 | 1 | |a Pian, Brooke |e verfasserin |4 aut | |
| 700 | 1 | |a Greetham, Darren |e verfasserin |4 aut | |
| 700 | 1 | |a Marecos-Ortiz, Sabrina |e verfasserin |4 aut | |
| 700 | 1 | |a Dickman, Mark J |e verfasserin |4 aut | |
| 700 | 1 | |a Lidbury, Ian D E A |e verfasserin |4 aut | |
| 700 | 1 | |a Lovering, Andrew L |e verfasserin |4 aut | |
| 700 | 1 | |a Barstow, Buz M |e verfasserin |4 aut | |
| 700 | 1 | |a Mesnage, Stéphane |e verfasserin |4 aut | |
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