PMID:7851435
| Citation |
Rossmann, R, Maier, T, Lottspeich, F and Böck, A (1995) Characterisation of a protease from Escherichia coli involved in hydrogenase maturation. Eur. J. Biochem. 227:545-50 |
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| Abstract |
The large subunits of nickel-containing hydrogenases are synthesised in a precursor form which, after nickel incorporation, is processed by proteolytic cleavage at the C-terminal end. The protease involved in processing of HycE, the large subunit of hydrogenase 3 from Escherichia coli, was purified by three chromatographic steps to apparent homogeneity. Its gene was identified by using a hybridisation probe generated by PCR with oligonucleotide primers the sequence of which was derived from the N-terminal and internal amino acid sequences. Determination of the nucleotide sequence showed that the gene is located distally and as a hitherto uncharacterised gene within the hyc operon, coding for hydrogenase 3 components. It was designated hycI. The HycI protease has a molecular mass of 17 kDa and is a monomer. Its cleavage reaction is not inhibited by conventional inhibitors of serine and metalloproteases, which correlates with the fact that the sequence does not contain signature motifs characteristic of serine-, metallo-, cysteine- or acid proteases. Homologous genes are present in other transcriptional units coding for hydrogenases. |
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| Keywords |
Amino Acid Sequence; Base Sequence; DNA, Bacterial; Endopeptidases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Hydrogenase/metabolism; Molecular Sequence Data; Protein Processing, Post-Translational; Sequence Homology, Amino Acid |
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