Phototropin Interactions with SUMO Proteins.

Arabidopsis / genetics Arabidopsis Proteins / genetics Chloroplasts / metabolism Escherichia coli / genetics Ligases / genetics Lysine / metabolism Mutation Phototropism / genetics Plant Leaves / genetics Plants, Genetically Modified Protein Serine-Threonine Kinases / genetics Seedlings / genetics Small Ubiquitin-Related Modifier Proteins / genetics Sumoylation
Arabidopsis Blue light Chloroplast movements Phototropin Phototropism Sumoylation

Journal

Plant & cell physiology
ISSN: 1471-9053
Titre abrégé: Plant Cell Physiol
Pays: Japan
ID NLM: 9430925

Informations de publication

Date de publication:
24 Sep 2021
Historique:
received: 10 08 2020
accepted: 10 02 2021
pubmed: 18 2 2021
medline: 21 10 2021
entrez: 17 2 2021
Statut: ppublish

Résumé

The disruption of the sumoylation pathway affects processes controlled by the two phototropins (phots) of Arabidopsis thaliana, phot1 and phot2. Phots, plant UVA/blue light photoreceptors, regulate growth responses and fast movements aimed at optimizing photosynthesis, such as phototropism, chloroplast relocations and stomatal opening. Sumoylation is a posttranslational modification, consisting of the addition of a SUMO (SMALL UBIQUITIN-RELATED MODIFIER) protein to a lysine residue in the target protein. In addition to affecting the stability of proteins, it regulates their activity, interactions and subcellular localization. We examined physiological responses controlled by phots, phototropism and chloroplast movements, in sumoylation pathway mutants. Chloroplast accumulation in response to both continuous and pulse light was enhanced in the E3 ligase siz1 mutant, in a manner dependent on phot2. A significant decrease in phot2 protein abundance was observed in this mutant after blue light treatment both in seedlings and mature leaves. Using plant transient expression and yeast two-hybrid assays, we found that phots interacted with SUMO proteins mainly through their N-terminal parts, which contain the photosensory LOV domains. The covalent modification in phots by SUMO was verified using an Arabidopsis sumoylation system reconstituted in bacteria followed by the mass spectrometry analysis. Lys 297 was identified as the main target of SUMO3 in the phot2 molecule. Finally, sumoylation of phot2 was detected in Arabidopsis mature leaves upon light or heat stress treatment.

Identifiants

DOI: 10.1093/pcp/pcab027 PMID: 33594440 PMC: PMC8462379
pubmed: 33594440
pii: 6140784
doi: 10.1093/pcp/pcab027
pmc: PMC8462379
doi:

Substances chimiques

Arabidopsis Proteins 0
PHOT2 protein, Arabidopsis 0
SUM1 protein, Arabidopsis 0
SUM2 protein, Arabidopsis 0
Small Ubiquitin-Related Modifier Proteins 0
NPH1 protein, Arabidopsis EC 2.7.11.1
Protein Serine-Threonine Kinases EC 2.7.11.1
Ligases EC 6.-
SIZ1 protein, Arabidopsis EC 6.3.2.-
Lysine K3Z4F929H6

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

693-707

Subventions

Organisme : The Polish National Science Centre
ID : UMO-2011/01/B/NZ3/02160 to H.G.
Organisme : European Regional Development Fund
ID : POIG.02.01.00-12-167/08
Organisme : Excellence Initiative -Research University

Informations de copyright

© The Author(s) 2021. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists.

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Auteurs

Justyna Łabuz (J)

Laboratory of Photobiology, Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.
ORCID: 0000-0002-2612-1658

Olga Sztatelman (O)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, Warszawa 02-106, Poland.

Dominika Jagiełło-Flasińska (D)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.

Paweł Hermanowicz (P)

Laboratory of Photobiology, Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.

Aneta Bażant (A)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.

Agnieszka Katarzyna Banaś (AK)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.
ORCID: 0000-0002-4029-4184

Filip Bartnicki (F)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.

Aleksandra Giza (A)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.

Anna Kozłowska (A)

Laboratory of Photobiology, Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.

Hanna Lasok (H)

Laboratory of Photobiology, Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.

Ewa Sitkiewicz (E)

Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, Warszawa 02-106, Poland.

Weronika Krzeszowiec (W)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.

Halina Gabryś (H)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.

Wojciech Strzałka (W)

Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków 30-387, Poland.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Viridiplantae › Streptophyta › Embryophyta › Tracheobionta › Magnoliopsida › Brassicaceae › Arabidopsis › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines végétales › Protéines d'Arabidopsis › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Plastes › Chloroplastes › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Bactéries › Proteobacteria › Gammaproteobacteria › Enterobacteriaceae › Escherichia › Escherichia coli › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés essentiels › Lysine › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Phénomènes génétiques › Variation génétique › Mutation › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Phénomènes physiologiques des plantes › Tropisme › Phototropisme › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Structures de plante › Parties aériennes de plante › Feuilles de plante › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Stades d'organismes › Organismes génétiquement modifiés › Végétaux génétiquement modifiés › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Eucaryotes › Plantes › Plant › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Ubiquitines › Petites protéines modificatrices apparentées à l'ubiquitine › Phototropin Interactions with SUMO Proteins.
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Ubiquitination › Sumoylation › Phototropin Interactions with SUMO Proteins.