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Literature summary for 2.7.11.1 extracted from

  • Trotta, A.; Suorsa, M.; Rantala, M.; Lundin, B.; Aro, E.
    Serine and threonine residues of plant STN7 kinase are differentially phosphorylated upon changing light conditions and specifically influence the activity and stability of the kinase (2016), Plant J., 87, 484-494 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
cytochrome b6f activation of STN7 via binding of plastoquinol to the cytochrome b6f (Cyt b6f) complex Arabidopsis thaliana

General Stability

General Stability Organism
serine and threonine residues of plant STN7 kinase are differentially phosphorylated upon changing light conditions and specifically influence the activity and stability of the kinase Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
DTT
-
Arabidopsis thaliana
additional information the enzyme is inhibited by high light Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid membrane
-
Arabidopsis thaliana 42651
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + light-harvesting complex II Arabidopsis thaliana
-
ADP + phospho-light-harvesting complex II
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein STN7 possesses one serine, Ser526 in NALAS526ALR, and two threonine phosphosites, Thr537 and Thr541 in T537VT539ET541IDEISDGR, at the C-terminus. The latter are found in several forms, besides the nonphosphorylated and phosphorylated forms, it is found as mis-cleaved peptides on both the N-terminus (LVKTVTETIDEISDGR) and the C-terminus (TVTETIDEISDGRK). Phosphorylation of the Thr residues protects STN7 against degradation in darkness, low light and red light, whereas increasing light intensity and far red illumination decrease phosphorylation and induce STN7 degradation. Ser phosphorylation, in turn, occurs under red and low intensity white light, coinciding with the client protein (LHCII) phosphorylation. Ser526 is detected only in two forms (nonphosphorylated and phosphorylated). Ser phosphorylation and activation of the STN7 kinase for subsequent LHCII phosphorylation are heavily affected by pre-illumination conditions. Transitions between the three activity states of the STN7 kinase (deactivated in darkness and far red light, activated in low and red light, inhibited in high light) are shown to modulate the phosphorylation of the STN7 Ser and Thr residues independently of each other. Detailed of phosphorylation regulation and metabolism, overview Arabidopsis thaliana

Purification (Commentary)

Purification (Comment) Organism
preparation of native thylakoids Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + light-harvesting complex II
-
Arabidopsis thaliana ADP + phospho-light-harvesting complex II
-
?

Synonyms

Synonyms Comment Organism
serine/threonine-protein kinase7
-
Arabidopsis thaliana
STN7
-
Arabidopsis thaliana
STN7 kinase
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
ATP
-
Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function STN7 kinase catalyzes the phosphorylation of the globally most common membrane proteins, the light-harvesting complex II (LHCII) in plant chloroplasts. Phosphorylation of the enzyme's Thr residues protects STN7 against degradation in darkness, low light and red light, whereas increasing light intensity and far red illumination decrease phosphorylation and induce STN7 degradation. Ser phosphorylation, in turn, occurs under red and low intensity white light, coinciding with the client protein (LHCII) phosphorylation. Ser phosphorylation and activation of the STN7 kinase for subsequent LHCII phosphorylation are heavily affected by pre-illumination conditions. Transitions between the three activity states of the STN7 kinase (deactivated in darkness and far red light, activated in low and red light, inhibited in high light) are shown to modulate the phosphorylation of the STN7 Ser and Thr residues independently of each other. Such dynamic regulation of STN7 kinase phosphorylation is crucial for plant growth and environmental acclimation. Exposure of plants to high light (HL) intensities leads to LHCII dephosphorylation by phosphatase TAP38/PPH1. Detailed of phosphorylation regulation and metabolism, overview Arabidopsis thaliana