Evidence map›Paper›PMID 33078277›Full record

ArticlePlant molecular biology2021

Genes encoding lipid II flippase MurJ and peptidoglycan hydrolases are required for chloroplast division in the moss Physcomitrella patens.

Hanae Utsunomiya, Nozomi Saiki, Hayato Kadoguchi, Masaya Fukudome, Satomi Hashimoto, Mami Ueda, Katsuaki Takechi, Hiroyoshi Takano

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Article in Plant molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 39% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
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  4. Molecular biology of mosses.Plant molecular biology · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Hanae UtsunomiyaGraduate School of Science and Technology, Kumamoto University, Kumamoto, 860-8555, Japan.
Nozomi SaikiGraduate School of Science and Technology, Kumamoto University, Kumamoto, 860-8555, Japan.
Hayato KadoguchiFaculty of Science, Kumamoto University, Kumamoto, 860-8555, Japan.
Masaya FukudomeFaculty of Science, Kumamoto University, Kumamoto, 860-8555, Japan.
Satomi HashimotoFaculty of Science, Kumamoto University, Kumamoto, 860-8555, Japan.
Mami UedaFaculty of Science, Kumamoto University, Kumamoto, 860-8555, Japan.
Katsuaki TakechiFaculty of Advanced Science and Technology, Kumamoto University, Kumamoto, 860-8555, Japan. ktakechi@kumamoto-u.ac.jp.
Hiroyoshi TakanoFaculty of Advanced Science and Technology, Kumamoto University, Kumamoto, 860-8555, Japan. takano@kumamoto-u.ac.jp.ORCID http://orcid.org/0000-0003-4720-5057
Kumamoto Health Science University · JPKumamoto University · JP

Funding

the Japan Society for the Promotion of Science 17H03701
6 · The paper itself

Abstract

key messageHomologous 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.

Indexed as

BryopsidaChloroplastsElectrophoresis, Polyacrylamide GelGene Expression Regulation, PlantGene Knockout TechniquesGreen Fluorescent ProteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanPhospholipid Transfer ProteinsPlant ProteinsPlants, Genetically ModifiedRecombinant Fusion ProteinsReverse Transcriptase Polymerase Chain ReactionUridine Diphosphate N-Acetylmuramic AcidGreen Fluorescent Proteinsmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanPhospholipid Transfer ProteinsPlant ProteinsRecombinant Fusion ProteinsUridine Diphosphate N-Acetylmuramic AcidChloroplast divisionLipid II flippaseLytic transglycosylasePeptidasePhyscomitrella patens

Identifiers

PMID33078277
OpenAlexW3093178645

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.