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Plant peptidoglycan precursor biosynthesis : conservation between moss chloroplasts and Gram-negative bacteria
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Dowson, Amanda J., Lloyd, Adrian J., Cuming, Andrew C., Roper, David I., Frigerio, Lorenzo and Dowson, Christopher G. (2022) Plant peptidoglycan precursor biosynthesis : conservation between moss chloroplasts and Gram-negative bacteria. Plant Physiology, 190 (1). pp. 165-179. doi:10.1093/plphys/kiac176
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WRAP-Plant-peptidoglycan-precursor-biosynthesis-conservation-between-moss-chloroplasts-and-Gram-negative-bacteria-Dowson-22.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (1384Kb) | Preview |
Official URL: http://dx.doi.org/10.1093/plphys/kiac176
Abstract
Accumulating evidence suggests that peptidoglycan, consistent with a bacterial cell wall, is synthesized around the chloroplasts of many photosynthetic eukaryotes, from glaucophyte algae to early-diverging land plants including pteridophyte ferns, but the biosynthetic pathway has not been demonstrated. Here, we employed mass spectrometry and enzymology in a two-fold approach to characterize the synthesis of peptidoglycan in chloroplasts of the moss Physcomitrium (Physcomitrella) patens. To drive the accumulation of peptidoglycan pathway intermediates, P. patens was cultured with the antibiotics fosfomycin, D-cycloserine, and carbenicillin, which inhibit key peptidoglycan pathway proteins in bacteria. Mass spectrometry of the trichloroacetic acid-extracted moss metabolome revealed elevated levels of five of the predicted intermediates from uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) through the uridine diphosphate N-acetylmuramic acid (UDP-MurNAc)-D,L-diaminopimelate (DAP)-pentapeptide. Most Gram-negative bacteria, including cyanobacteria, incorporate meso-diaminopimelic acid (D,L-DAP) into the third residue of the stem peptide of peptidoglycan, as opposed to L-lysine, typical of most Gram-positive bacteria. To establish the specificity of D,L-DAP incorporation into the P. patens precursors, we analyzed the recombinant protein UDP-N-acetylmuramoyl-L-alanyl-D-glutamate–2,6-diaminopimelate ligase (MurE) from both P. patens and the cyanobacterium Anabaena sp. (Nostoc sp. strain PCC 7120). Both ligases incorporated D,L-DAP in almost complete preference to L-Lys, consistent with the mass spectrophotometric data, with catalytic efficiencies similar to previously documented Gram-negative bacterial MurE ligases. We discuss how these data accord with the conservation of active site residues common to DL-DAP-incorporating bacterial MurE ligases and of the probability of a horizontal gene transfer event within the plant peptidoglycan pathway.
| Item Type: | Journal Article | |||||||||||||||
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| Subjects: | Q Science > QK Botany Q Science > QP Physiology Q Science > QR Microbiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||||||||
| Library of Congress Subject Headings (LCSH): | Physcomitrella patens, Peptidoglycans, Chloroplasts, Gram-negative bacteria | |||||||||||||||
| Journal or Publication Title: | Plant Physiology | |||||||||||||||
| Publisher: | Oxford University Press | |||||||||||||||
| ISSN: | 1532-2548 | |||||||||||||||
| Official Date: | September 2022 | |||||||||||||||
| Dates: |
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| Volume: | 190 | |||||||||||||||
| Number: | 1 | |||||||||||||||
| Page Range: | pp. 165-179 | |||||||||||||||
| DOI: | 10.1093/plphys/kiac176 | |||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||
| Publication Status: | Published | |||||||||||||||
| Access rights to Published version: | Open Access | |||||||||||||||
| RIOXX Funder/Project Grant: |
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