Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli |
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Authors: | Frank Andreas Krone Goetz Westphal Jens Dirk Schwenn |
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Affiliation: | (1) Biochemistry of Plants, Faculty of Biology, Ruhr University Bochum, Universitätsstrasse 150, Postfach 102148, W-4630 Bochum 1, Germany |
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Abstract: | Summary The nucleotide sequence of the gene cysH from Escherichia coli K12 was determined. The open reading frame was 735 nucleotides in length; it was flanked by a repetitive palindromic sequence centred 36 nucleotides upstream of cysH and a terminator-like structure located 20 nucleotides downstream. CysH encoded a colypeptide of Mr 27927 consisting of 244 amino acids. The gene product was isolated as a homodimer exhibiting phospo-adenylylsulphate reductase (PAPS reductase) activity. The active enzyme was devoid of electron transferring cofactors and contained only one cysteine per subunit. Reduction of the enzyme by dithiols resulted in a shift of the apparent molecular weight from 44000 to 62000 without formation of an enzyme-thioredoxin complex.
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Keywords: | PAPS reductase cysH DNA sequence Gene product Phenotypic complementation Escherichia coli K12 |
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