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Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens

Class A penicillin-binding proteins (PBPs) are active in the final step of bacterial peptidoglycan biosynthesis. They possess a transglycosylase (TG) domain to polymerize the glycan chains and a transpeptidase (TP) domain to catalyze peptide cross-linking. We reported that knockout of the Pbp gene i...

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Autores principales: TAKAHASHI, Yoshiko, TAKECHI, Katsuaki, TAKIO, Susumu, TAKANO, Hiroyoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japan Academy 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5328786/
https://www.ncbi.nlm.nih.gov/pubmed/27941308
http://dx.doi.org/10.2183/pjab.92.499
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author TAKAHASHI, Yoshiko
TAKECHI, Katsuaki
TAKIO, Susumu
TAKANO, Hiroyoshi
author_facet TAKAHASHI, Yoshiko
TAKECHI, Katsuaki
TAKIO, Susumu
TAKANO, Hiroyoshi
author_sort TAKAHASHI, Yoshiko
collection PubMed
description Class A penicillin-binding proteins (PBPs) are active in the final step of bacterial peptidoglycan biosynthesis. They possess a transglycosylase (TG) domain to polymerize the glycan chains and a transpeptidase (TP) domain to catalyze peptide cross-linking. We reported that knockout of the Pbp gene in the moss Physcomitrella patens (ΔPpPbp) results in a macrochloroplast phenotype by affecting plastid division. Here, expression of PpPBP-GFP in ΔPpPbp restored the wild-type phenotype and GFP fluorescence was observed mainly in the periphery of each chloroplast. Stable transformants expressing Anabaena PBP with the plastid-targeting sequence, or PpPBP replacing the Anabaena TP domain exhibited partial recovery, while chloroplast number was recovered to that of wild-type plants in the transformant expressing PpPBP replacing the Anabaena TG domain. Transient expression experiments with site-directed mutagenized PpPBP showed that mutations in the conserved amino acids in both domains interfered with phenotype recovery. These results suggest that both TG and TP functions are essential for function of PpPBP in moss chloroplast division.
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spelling pubmed-53287862017-03-21 Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens TAKAHASHI, Yoshiko TAKECHI, Katsuaki TAKIO, Susumu TAKANO, Hiroyoshi Proc Jpn Acad Ser B Phys Biol Sci Original Article Class A penicillin-binding proteins (PBPs) are active in the final step of bacterial peptidoglycan biosynthesis. They possess a transglycosylase (TG) domain to polymerize the glycan chains and a transpeptidase (TP) domain to catalyze peptide cross-linking. We reported that knockout of the Pbp gene in the moss Physcomitrella patens (ΔPpPbp) results in a macrochloroplast phenotype by affecting plastid division. Here, expression of PpPBP-GFP in ΔPpPbp restored the wild-type phenotype and GFP fluorescence was observed mainly in the periphery of each chloroplast. Stable transformants expressing Anabaena PBP with the plastid-targeting sequence, or PpPBP replacing the Anabaena TP domain exhibited partial recovery, while chloroplast number was recovered to that of wild-type plants in the transformant expressing PpPBP replacing the Anabaena TG domain. Transient expression experiments with site-directed mutagenized PpPBP showed that mutations in the conserved amino acids in both domains interfered with phenotype recovery. These results suggest that both TG and TP functions are essential for function of PpPBP in moss chloroplast division. The Japan Academy 2016-12-09 /pmc/articles/PMC5328786/ /pubmed/27941308 http://dx.doi.org/10.2183/pjab.92.499 Text en © 2016 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
TAKAHASHI, Yoshiko
TAKECHI, Katsuaki
TAKIO, Susumu
TAKANO, Hiroyoshi
Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens
title Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens
title_full Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens
title_fullStr Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens
title_full_unstemmed Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens
title_short Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens
title_sort both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in physcomitrella patens
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5328786/
https://www.ncbi.nlm.nih.gov/pubmed/27941308
http://dx.doi.org/10.2183/pjab.92.499
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