Redefining reductive sulfate assimilation in higher plants: a role for APS reductase, a new member of the thioredoxin superfamily?

John Langford Wray, EI Campbell, MA Roberts, JF Gutierrez-Marcos

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

The reaction steps leading from the intermediate adenosine 5'-phosphosulfate (APS) to sulfide within the higher plant reductive sulfate assimilation pathway are the subject of controversy. Two pathways have been proposed: a 'bound intermediate' pathway in which the sulfo group of APS is first transferred by APS sulfotransferase to a carrier molecule to form a bound sulfite intermediate and is then further reduced by thiosulfonate reductase to bound sulfide; and a 'free intermediate' pathway in which APS is further activated to 3'-phosphoadenosine 5'-phosphosulfate (PAPS) by APS kinase followed by reduction of the sulfo group to free sulfite by PAPS reductase. Sulfite is then reduced to foe sulfide by sulfite reductase. Sulfide, either free or bound, is then incorporated into organic form (as cysteine) by the enzyme O-acetylserine (thiol) lyase. In order to better characterize the pathway we attempted to clone PAPS reductase cDNAs by functional complementation of an Escherichia coli cysH mutant to prototrophy. We found no evidence for PAPS reductase cDNAs but did identify cDNAs that encode a small family of novel, chloroplast-localized proteins with APS reductase activity that are new members of the thioredoxin superfamily. We show here that the thioredoxin domain of these proteins is functional. We speculate that rather than proceeding via either of the pathways proposed above, reductive sulfate assimilation proceeds via the reduction of APS to sulfite by APS reductase and the subsequent reduction of sulfite to sulfide by sulfite reductase. In this scheme the product of the APS kinase reaction, PAPS, is not a direct intermediate in the pathway but rather acts as a substrate fur sulfotransferase action and perhaps as a store of activated sulfate that can be returned to the pathway as APS via phosphohydrolase action on PAPS. Interactions between enzyme isoforms within the chloroplast stroma may bring about substrate channeling of APS and contribute to the partitioning of APS between sulfotransferase reactions an the one hand and the synthesis of cysteine and related metabolites via the reductive sulfate assimilation pathway on the other. (C) 1998 Elsevier Science ireland Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)153-167
Number of pages15
JournalChemico-Biological Interactions
Volume109
Publication statusPublished - 20 Feb 1998

Keywords

  • higher plants
  • reductive sulfate assimilation
  • APS reductase
  • ADENOSINE 5'-PHOSPHOSULFATE SULFOTRANSFERASE
  • FERREDOXIN-SULFITE REDUCTASE
  • AMINO-ACID-SEQUENCE
  • ESCHERICHIA-COLI
  • ARABIDOPSIS-THALIANA
  • PARTIAL-PURIFICATION
  • PAPS-REDUCTASE
  • 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE
  • SACCHAROMYCES-CEREVISIAE
  • ENZYME

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