Evidence map›Paper›PMID 39098962›Full record

ArticleJournal of plant research2024

SENSITIVE TO FREEZING2 is crucial for growth of Marchantia polymorpha under acidic conditions.

Shinsuke Shimizu, Koichi Hori, Kimitsune Ishizaki, Hiroyuki Ohta, Mie Shimojima

Abstract read
In one paragraph

Article in Journal of plant research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Shinsuke ShimizuSchool of Life Science and Technology, Tokyo Institute of Technology, 4259-B-65, Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Kanagawa, Japan.
Koichi HoriSchool of Life Science and Technology, Tokyo Institute of Technology, 4259-B-65, Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Kanagawa, Japan.ORCID http://orcid.org/0000-0002-0530-181X
Kimitsune IshizakiGraduate School of Science, Kobe University, Kobe, Japan.ORCID http://orcid.org/0000-0003-0504-8196
Hiroyuki OhtaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259-B-65, Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Kanagawa, Japan.ORCID http://orcid.org/0000-0002-1816-7912
Mie ShimojimaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259-B-65, Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Kanagawa, Japan. shimojima.m.aa@m.titech.ac.jp.ORCID http://orcid.org/0000-0003-3172-8638

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Land plants have evolved many systems to adapt to a wide range of environmental stresses. In seed plants, oligogalactolipid synthesis is involved in tolerance to freezing and dehydration, but it has not been analyzed in non-vascular plants. Here we analyzed trigalactosyldiacylglycerol (TGDG) synthesis in Marchantia polymorpha. TGDG is synthesized by galactolipid: galactolipid galactosyltransferase [GGGT; SENSITIVE TO FREEZING2 (SFR2) in Arabidopsis]. We analyzed the subcellular localization and GGGT activity of two M. polymorpha SFR2 homologs (MpGGGT1 and MpGGGT2, each as a GFP-fusion protein) using a transient expression system in Nicotiana benthamiana leaves and found that MpGGGT1-GFP localized in the chloroplast envelope membrane. We produced mutants Mpgggt1 and Mpgggt2 and found that TGDG did not accumulate in Mpgggt1 upon treatment of the thallus with acetic acid. Moreover, growth of Mpgggt1 mutants was impaired by acetic acid treatment. Microscopy revealed that the acetic acid treatment of M. polymorpha plants damaged intracellular membranes. The fact that the effect was similar for wild-type and Mpgggt1 plants suggested that MpGGGT has a role in recovery from damage. These results indicate that MpGGGT plays a crucial role in M. polymorpha growth under conditions of acid stress, which may have been encountered during the ancient terrestrial colonization of plants.

Indexed as

MarchantiaArabidopsis Proteinsbeta-GlucosidaseFreezingGalactosyltransferasesGene Expression Regulation, PlantMutationNicotianaPlant LeavesPlant ProteinsStress, PhysiologicalArabidopsis Proteinsbeta-GlucosidaseGalactosyltransferasesPlant ProteinsSFR2 protein, ArabidopsisAcidic stressGGGTMarchantia polymorphaOligogalactolipidSFR2Trigalactosyldiacylglycerol

Identifiers

PMID39098962
PMCPMC11525325

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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.