Genes encoding lipid II flippase MurJ and peptidoglycan hydrolases are required for chloroplast division in the moss Physcomitrella patens.
Bryopsida
/ genetics
Chloroplasts
/ genetics
Electrophoresis, Polyacrylamide Gel
Gene Expression Regulation, Plant
Gene Knockout Techniques
Green Fluorescent Proteins
/ genetics
N-Acetylmuramoyl-L-alanine Amidase
/ genetics
Peptidoglycan
/ metabolism
Phospholipid Transfer Proteins
/ genetics
Plant Proteins
/ genetics
Plants, Genetically Modified
Recombinant Fusion Proteins
/ genetics
Reverse Transcriptase Polymerase Chain Reaction
Uridine Diphosphate N-Acetylmuramic Acid
/ analogs & derivatives
Chloroplast division
Lipid II flippase
Lytic transglycosylase
Peptidase
Physcomitrella patens
Journal
Plant molecular biology
ISSN: 1573-5028
Titre abrégé: Plant Mol Biol
Pays: Netherlands
ID NLM: 9106343
Informations de publication
Date de publication:
Nov 2021
Nov 2021
Historique:
received:
24
07
2020
accepted:
02
10
2020
pubmed:
21
10
2020
medline:
21
12
2021
entrez:
20
10
2020
Statut:
ppublish
Résumé
Homologous genes for the peptidoglycan precursor flippase MurJ, and peptidoglycan hydrolases: lytic transglycosylase MltB, and DD-carboxypeptidase VanY are required for chloroplast division in the moss Physcomitrella patens. The moss Physcomitrella patens is used as a model plant to study plastid peptidoglycan biosynthesis. In bacteria, MurJ flippase transports peptidoglycan precursors from the cytoplasm to the periplasm. In this study, we identified a MurJ homolog (PpMurJ) in the P. patens genome. Bacteria employ peptidoglycan degradation and recycling pathways for cell division. We also searched the P. patens genome for genes homologous to bacterial peptidoglycan hydrolases and identified genes homologous for the lytic transglycosylase mltB, N-acetylglucosaminidase nagZ, and LD-carboxypeptidase ldcA in addition to a putative DD-carboxypeptidase vanY reported previously. Moreover, we found a ß-lactamase-like gene (Pplactamase). GFP fusion proteins with either PpMltB or PpVanY were detected in the chloroplasts, whereas fusion proteins with PpNagZ, PpLdcA, or Pplactamase localized in the cytoplasm. Experiments seeking PpMurJ-GFP fusion proteins failed. PpMurJ gene disruption in P. patens resulted in the appearance of macrochloroplasts in protonemal cells. Compared with the numbers of chloroplasts in wild-type plants (38.9 ± 4.9), PpMltB knockout and PpVanY knockout had lower numbers of chloroplasts (14.3 ± 6.7 and 28.1 ± 5.9, respectively). No differences in chloroplast numbers were observed after PpNagZ, PpLdcA, or Pplactamase single-knockout. Chloroplast numbers in PpMltB/PpVanY double-knockout cells were similar to those in PpMltB single-knockout cells. Zymogram analysis of the recombinant PpMltB protein revealed its peptidoglycan hydrolase activity. Our results imply that PpMurJ, PpMltB and PpVanY play a critical role in chloroplast division in the moss P. patens.
Identifiants
pubmed: 33078277
doi: 10.1007/s11103-020-01081-0
pii: 10.1007/s11103-020-01081-0
doi:
Substances chimiques
Peptidoglycan
0
Phospholipid Transfer Proteins
0
Plant Proteins
0
Recombinant Fusion Proteins
0
Uridine Diphosphate N-Acetylmuramic Acid
0
muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol
0
Green Fluorescent Proteins
147336-22-9
N-Acetylmuramoyl-L-alanine Amidase
EC 3.5.1.28
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
405-415Subventions
Organisme : the Japan Society for the Promotion of Science
ID : 17H03701
Informations de copyright
© 2020. Springer Nature B.V.
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