Redox regulation of ATP sulfurylase in microalgae

0468470 - MBÚ 2017 RIV US eng J - Článek v odborném periodiku
Prioretti, L. - Lebrun, R. - Gontero, B. - Giordano, Mario
Redox regulation of ATP sulfurylase in microalgae.
Biochemical and Biophysical Research Communications. Roč. 478, č. 4 (2016), s. 1555-1562. ISSN 0006-291X. E-ISSN 1090-2104
Institucionální podpora: RVO:61388971
Klíčová slova: ATP sulfurylase * cysteine * Sulfur metabolism
Kód oboru RIV: EE - Mikrobiologie, virologie
Impakt faktor: 2.466, rok: 2016

ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms. An ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines; five of them are conserved, but only one in the same position as ATPS-A. We investigated the role of cysteines on the regulation of the different algal enzymes. We found that the activity of ATPS-B from four different microorganisms was enhanced when reduced and decreased when oxidized. The LC-MS/MS analysis of the ATPS-B from the marine diatom Thalassiosira pseudonana showed that the residue Cys-247 was presumably involved in the redox regulation. The absence of this residue in the ATPS-A of the freshwater cyanobacterium Synechocystis sp. instead, was consistent with its lack of regulation. Some other conserved cysteine residues in the ATPS from T. pseduonana and not in Synechocystis sp. were accessible to redox agents and possibly play a role in the enzyme regulation. Furthermore, the fact that oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. (
Trvalý link: http://hdl.handle.net/11104/0267391