Redox regulation of ATP sulfurylase in microalgae
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00468470" target="_blank" >RIV/61388971:_____/16:00468470 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.bbrc.2016.08.151" target="_blank" >http://dx.doi.org/10.1016/j.bbrc.2016.08.151</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbrc.2016.08.151" target="_blank" >10.1016/j.bbrc.2016.08.151</a>
Alternative languages
Result language
angličtina
Original language name
Redox regulation of ATP sulfurylase in microalgae
Original language description
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. (
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochemical and Biophysical Research Communications
ISSN
0006-291X
e-ISSN
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Volume of the periodical
478
Issue of the periodical within the volume
4
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
1555-1562
UT code for WoS article
000384390200011
EID of the result in the Scopus database
2-s2.0-84992107986