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Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli

✍ Scribed by Krone, Frank Andreas ;Westphal, Goetz ;Schwenn, Jens Dirk

Publisher
Springer
Year
1991
Tongue
English
Weight
855 KB
Volume
225
Category
Article
ISSN
0026-8925

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✦ Synopsis

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 polypeptide of Mr 27927 consisting of 244 amino acids. The gene product was isolated as a homodimer exhibiting phospho-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 44,000 to 62,000 without formation of an enzyme-thioredoxin complex.

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