Pubblicazioni

Identification of pH-sensing Sites in the Light Harvesting Complex Stress-related 3 Protein Essential for Triggering Non-photochemical Quenching in Chlamydomonas reinhardtii  (2016)

Autori:
Ballottari, Matteo; Truong, Thuy B; De Re, Eleonora; Erickson, Erika; Stella, Giulio Rocco; Fleming, Graham R; Bassi, Roberto; Niyogi, Krishna K.
Titolo:
Identification of pH-sensing Sites in the Light Harvesting Complex Stress-related 3 Protein Essential for Triggering Non-photochemical Quenching in Chlamydomonas reinhardtii
Anno:
2016
Tipologia prodotto:
Articolo in Rivista
Tipologia ANVUR:
Articolo su rivista
Lingua:
Inglese
Formato:
A Stampa
Referee:
Nome rivista:
JBC
ISSN Rivista:
0021-9258
N° Volume:
291
Numero o Fascicolo:
14
Intervallo pagine:
7334-7346
Parole chiave:
fluorescence; non-photochemical quenching; photoprotection; photosynthesis; photosynthetic pigment; photosystem II; plant biochemistry; Chlamydomonas reinhardtii; Hydrogen-Ion Concentration; Light-Harvesting Protein Complexes; Mutagenesis, Site-Directed; Mutation, Missense; Thylakoids
Breve descrizione dei contenuti:
Light harvesting complex stress-related 3 (LHCSR3) is the protein essential for photoprotective excess energy dissipation (non-photochemical quenching, NPQ) in the model green algaChlamydomonas reinhardtii Activation of NPQ requires low pH in the thylakoid lumen, which is induced in excess light conditions and sensed by lumen-exposed acidic residues. In this work we have used site-specific mutagenesisin vivoandin vitrofor identification of the residues in LHCSR3 that are responsible for sensing lumen pH. Lumen-exposed protonatable residues, aspartate and glutamate, were mutated to asparagine and glutamine, respectively. By expression in a mutant lacking all LHCSR isoforms, residues Asp(117), Glu(221), and Glu(224)were shown to be essential for LHCSR3-dependent NPQ induction inC. reinhardtii Analysis of recombinant proteins carrying the same mutations refoldedin vitrowith pigments showed that the capacity of responding to low pH by decreasing the fluorescence lifetime, present in the wild-type protein, was lost. Consistent with a role in pH sensing, the mutations led to a substantial reduction in binding the NPQ inhibitor dicyclohexylcarbodiimide.
Id prodotto:
94852
Handle IRIS:
11562/954290
ultima modifica:
12 novembre 2022
Citazione bibliografica:
Ballottari, Matteo; Truong, Thuy B; De Re, Eleonora; Erickson, Erika; Stella, Giulio Rocco; Fleming, Graham R; Bassi, Roberto; Niyogi, Krishna K., Identification of pH-sensing Sites in the Light Harvesting Complex Stress-related 3 Protein Essential for Triggering Non-photochemical Quenching in Chlamydomonas reinhardtii «JBC» , vol. 291 , n. 142016pp. 7334-7346

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Progetti Collegati
Titolo Dipartimento Responsabili
PRIN 2012 Miglioramento della produzione di biocombustibili e molecole ad elevato valore aggiunto in alghe unicellulari Dipartimento Biotecnologie Matteo Ballottari
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