Dissimilatory ATP sulfurylase from the hyperthermophilic sulfate reducer Archaeoglobus fulgidus belongs to the group of homo-oligomeric ATP sulfurylases
- 作者：Sperling ; Detlef ; Kappler ; Ulrike ; Wynen ; Astrid ; Dahl ; Christiane ; Trü ; per ; Hans G.
- 关键词：Archaeoglobus fulgidus ; Hyperthermophilic archaea ; Adenosine triphosphate sulfurylase ; Adenosine-5&prime ; -phosphosulfate reductase ; Dissimilatory sulfate reduction ; Heterologous expression
- 刊名：FEMS Microbiology Letters
- 出版年：1998
- 期刊代码：34_03781097
- 类别：imm
- 出版时间：May 15, 1998
- 卷：162
- 期：2
- 页码：257-264
- 文件大小：401 K
摘要
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.