Dissimilatory ATP sulfurylase from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus belongs to the group of homo-oligomeric ATP sulfurylases

Sperling, Detlef, Kappler, Ulrike, Wynen, Astrid, Dahl, Christiane and Trüper, Hans G. (1998) Dissimilatory ATP sulfurylase from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus belongs to the group of homo-oligomeric ATP sulfurylases. FEMS Microbiology Letters, 162 2: 257-264. doi:10.1111/j.1574-6968.1998.tb13007.x


Author Sperling, Detlef
Kappler, Ulrike
Wynen, Astrid
Dahl, Christiane
Trüper, Hans G.
Title Dissimilatory ATP sulfurylase from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus belongs to the group of homo-oligomeric ATP sulfurylases
Formatted title
Dissimilatory ATP sulfurylase from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus belongs to the group of homo-oligomeric ATP sulfurylases
Journal name FEMS Microbiology Letters   Check publisher's open access policy
ISSN 0378-1097
1574-6968
Publication date 1998
Sub-type Article (original research)
DOI 10.1111/j.1574-6968.1998.tb13007.x
Volume 162
Issue 2
Start page 257
End page 264
Total pages 8
Place of publication Oxford, UK
Publisher Blackwell Publishing
Language eng
Subject 060599 Microbiology not elsewhere classified
060107 Enzymes
Formatted abstract
In the hyperthermophilic sulfate reducer Archaeoglobus fulgidus DSM 4304T, two open reading frames (sat and ORF2) are located upstream of the aprBA genes encoding adenosine-5'-phosphosulfate (APS) reductase. sat-ORF2-aprBA probably form a transcriptional unit, since sat is preceded by putative promoter sequences and termination signals are found downstream of aprA. While the 117-residue ORF2 product does not show significant similarity to known proteins, the 456-residue, 52.78-kDa, sat-encoded polypeptide exhibits similarity to the homo-oligomeric adenosine triphosphate (ATP) sulfurylases from sulfur-oxidizing bacteria and from sulfate-assimilating bacteria and eukaryotes. Functional overexpression of sat in Escherichia coli proved that the encoded protein acts as an ATP sulfurylase. The recombinant protein was purified to homogeneity and found to be a homo-dimer. Comparison of sulfate and thiosulfate grown A. fulgidus revealed that ATP sulfurylase and APS reductase are constitutive enzymes. Distance matrix analyses allowed insights into the evolution of prokaryotic ATP sulfurylases.
Keyword Archaeoglobus fulgidus
Hyperthermophilic archaea
Adenosine triphosphate sulfurylase
Adenosine-5'-phosphosulfate reductase
Dissimilatory sulfate reduction
Heterologous expression
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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