info:eu-repo/semantics/article
Identification and characterization of ChlreSEX4, a novel glucan phosphatase from Chlamydomonas reinhardtii green alga
Fecha
2020-02Registro en:
Carrillo, Julieta Beatriz; Torresi, Florencia; Morales, Luisina Lourdes; Ricordi, Micaela; Gomez Casati, Diego Fabian; et al.; Identification and characterization of ChlreSEX4, a novel glucan phosphatase from Chlamydomonas reinhardtii green alga; Elsevier Science Inc.; Archives of Biochemistry and Biophysics; 680; 2-2020; 1-12
0003-9861
CONICET Digital
CONICET
Autor
Carrillo, Julieta Beatriz
Torresi, Florencia
Morales, Luisina Lourdes
Ricordi, Micaela
Gomez Casati, Diego Fabian
Busi, María Victoria
Martín, Mariana
Resumen
Chlamydomonas reinhardtii is the best known unicellular green alga model which has long been used to investigate all kinds of cellular processes, including starch metabolism. Here we identified and characterized a novel enzyme, ChlreSEX4, orthologous to glucan phosphatase SEX4 from Arabidopsis thaliana, that is capable of binding and dephosphorylating amylopectin in vitro. We also reported that cysteine 224 and tryptophan 305 residues are critical for enzyme catalysis and substrate binding. Furthermore, we verified that ChlreSEX4 gene is expressed in vivo and that glucan phosphatase activity is measurable in Chlamydomonas protein extracts. In view of the results presented, we suggest ChlreSEX4 as a functional phosphoglucan phosphatase from C. reinhardtii. Our data obtained so far contribute to understanding the phosphoglucan phosphatases evolutionary process in the green lineage and their role in starch reversible phosphorylation. In addition, this allows to position Chlamydomonas as a potential tool to obtain starches with different degrees of phosphorylation for industrial or biotechnological purposes.