About: Diversity and regulation of ATP sulfurylase in photosynthetic organisms     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
Description
  • ATP sulfurylase (AIRS) catalyzes the first committed step in the sulfate assimilation pathway, the activation of sulfate prior to its reduction. AIRS has been studied in only a few model organisms and even in these cases to a much smaller extent than the sulfate reduction and cysteine synthesis enzymes. This is possibly because the latter were considered of greater regulatory importance for sulfate assimilation. Recent evidences (reported in this paper) challenge this view and suggest that AIRS may have a crucial regulatory role in sulfate assimilation, at least in algae. In the ensuing text, we summarize the current knowledge on AIRS, with special attention to the processes that control its activity and gene(s) expression in algae. Special attention is given to algae AIRS proteins. The focus on algae is the consequence of the fact that a comprehensive investigation of AIRS revealed that the algal enzymes, especially those that are most likely involved in the pathway of sulfate reduction to cysteine, possess features that are not present in other organisms. Remarkably, algal AIRS proteins show a great diversity of isoforms and a high content of cysteine residues, whose positions are often conserved. According to the occurrence of cysteine residues, the AIRS of eukaryotic algae is closer to that of marine cyanobacteria of the genera Synechococcus and Prochlorococcus and is more distant from that of freshwater cyanobacteria. These characteristics might have evolved in parallel with the radiation of algae in the oceans and the increase of sulfate concentration in seawater.
  • ATP sulfurylase (AIRS) catalyzes the first committed step in the sulfate assimilation pathway, the activation of sulfate prior to its reduction. AIRS has been studied in only a few model organisms and even in these cases to a much smaller extent than the sulfate reduction and cysteine synthesis enzymes. This is possibly because the latter were considered of greater regulatory importance for sulfate assimilation. Recent evidences (reported in this paper) challenge this view and suggest that AIRS may have a crucial regulatory role in sulfate assimilation, at least in algae. In the ensuing text, we summarize the current knowledge on AIRS, with special attention to the processes that control its activity and gene(s) expression in algae. Special attention is given to algae AIRS proteins. The focus on algae is the consequence of the fact that a comprehensive investigation of AIRS revealed that the algal enzymes, especially those that are most likely involved in the pathway of sulfate reduction to cysteine, possess features that are not present in other organisms. Remarkably, algal AIRS proteins show a great diversity of isoforms and a high content of cysteine residues, whose positions are often conserved. According to the occurrence of cysteine residues, the AIRS of eukaryotic algae is closer to that of marine cyanobacteria of the genera Synechococcus and Prochlorococcus and is more distant from that of freshwater cyanobacteria. These characteristics might have evolved in parallel with the radiation of algae in the oceans and the increase of sulfate concentration in seawater. (en)
Title
  • Diversity and regulation of ATP sulfurylase in photosynthetic organisms
  • Diversity and regulation of ATP sulfurylase in photosynthetic organisms (en)
skos:prefLabel
  • Diversity and regulation of ATP sulfurylase in photosynthetic organisms
  • Diversity and regulation of ATP sulfurylase in photosynthetic organisms (en)
skos:notation
  • RIV/61388971:_____/14:00440799!RIV15-AV0-61388971
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I
http://linked.open...iv/cisloPeriodika
  • 597
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
  • Giordano, Mario
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 11918
http://linked.open...ai/riv/idVysledku
  • RIV/61388971:_____/14:00440799
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • sulfurylase; diversity; algae; cyanobacteria (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • CH - Švýcarská konfederace
http://linked.open...ontrolniKodProRIV
  • [50B0D003A6D5]
http://linked.open...i/riv/nazevZdroje
  • Frontiers in Plant Science
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 5
http://linked.open...iv/tvurceVysledku
  • Giordano, Mario
  • Gontero, B.
  • Hell, R.
  • Prioretti, L.
http://linked.open...ain/vavai/riv/wos
  • 000346919000001
issn
  • 1664-462X
number of pages
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 48 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software