The Presence of an Iron-Sulfur Cluster in Adenosine 5′-Phosphosulfate Reductase Separates Organisms Utilizing Adenosine 5′-Phosphosulfate and Phosphoadenosine 5′-Phosphosulfate for Sulfate Assimilation

Kopriva, Stanislav; Büchert, Thomas; Fritz, Günter; Suter, Marianne; Benda, Rüdiger; Schünemann, Volker; Koprivova, Anna; Schürmann, Peter; Trautwein, Alfred X.; Kroneck, Peter M. H.; Brunold, Christian (2002). The Presence of an Iron-Sulfur Cluster in Adenosine 5′-Phosphosulfate Reductase Separates Organisms Utilizing Adenosine 5′-Phosphosulfate and Phosphoadenosine 5′-Phosphosulfate for Sulfate Assimilation. Journal of biological chemistry, 277(24), pp. 21786-21791. American Society for Biochemistry and Molecular Biology 10.1074/jbc.M202152200

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It was generally accepted that plants, algae, and phototrophic bacteria use adenosine 5′-phosphosulfate (APS) for assimilatory sulfate reduction, whereas bacteria and fungi use phosphoadenosine 5′-phosphosulfate (PAPS). The corresponding enzymes, APS and PAPS reductase, share 25–30% identical amino acids. Phylogenetic analysis of APS and PAPS reductase amino acid sequences from different organisms, which were retrieved from the GenBankTM, revealed two clusters. The first cluster comprised known PAPS reductases from enteric bacteria, cyanobacteria, and yeast. On the other hand, plant APS reductase sequences were clustered together with many bacterial ones, including those fromPseudomonas and Rhizobium. The gene for APS reductase cloned from the APS-reducing cyanobacteriumPlectonema also clustered together with the plant sequences, confirming that the two classes of sequences represent PAPS and APS reductases, respectively. Compared with the PAPS reductase, all sequences of the APS reductase cluster contained two additional cysteine pairs homologous to the cysteine residues involved in binding an iron-sulfur cluster in plants. Mössbauer analysis revealed that the recombinant APS reductase from Pseudomonas aeruginosa contains a [4Fe-4S] cluster with the same characteristics as the plant enzyme. We conclude, therefore, that the presence of an iron-sulfur cluster determines the APS specificity of the sulfate-reducing enzymes and thus separates the APS- and PAPS-dependent assimilatory sulfate reduction pathways.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) > Stress Physiology (discontinued)
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS)

UniBE Contributor:

Suter, Marianne and Brunold, Christian

Subjects:

500 Science > 580 Plants (Botany)

ISSN:

0021-9258

Publisher:

American Society for Biochemistry and Molecular Biology

Language:

English

Submitter:

Peter Alfred von Ballmoos-Haas

Date Deposited:

30 Jan 2018 09:24

Last Modified:

23 Oct 2019 10:11

Publisher DOI:

10.1074/jbc.M202152200

PubMed ID:

11940598

BORIS DOI:

10.7892/boris.107365

URI:

https://boris.unibe.ch/id/eprint/107365

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