The sialidase gene from Clostridium septicum: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins
| Autor: | Beate Rothe, Bernd Rothe, Peter Roggentin, Roland Schauer |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Clostridium
DNA Bacterial Genetics chemistry.chemical_classification Base Sequence Molecular Sequence Data Restriction Mapping Nucleic acid sequence Neuraminidase Sequence alignment Biology Sialidase Conserved sequence Ribosomal binding site Amino acid Biochemistry chemistry Sequence Homology Nucleic Acid Escherichia coli Consensus sequence Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence |
| Zdroj: | Molecular and General Genetics MGG. :190-197 |
| ISSN: | 1432-1874 0026-8925 |
| DOI: | 10.1007/bf00273603 |
| Popis: | An oligonucleotide mixture corresponding to the codons for conserved and repeated amino acid sequences of bacterial sialidases (Roggentin et al. 1989) was used to clone a 4.3 kb PstI restriction fragment of Clostridium septicum DNA in Escherichia coli. The complete nucleotide sequence of the sialidase gene was determined from this fragment. The derived amino acid sequence corresponds to a protein of 110,000 Da. The ribosomal binding site and promoter-like consensus sequences were identified upstream from the putative ATG initiation codon. The molecular and immunological properties of the sialidase expressed by E. coli are similar to those of the sialidase as isolated from C. septicum. The newly synthesized protein is assumed to include a leader peptide of 26 amino acids. On sequence alignment, the sialidases from C. septicum, C. sordellii and C. perfringens show significant homologies. As in other bacterial sialidases, conserved amino acid sequences occur at four positions in the protein. Aside from the consensus sequences, only poor homology to other bacterial and viral sialidases was found. The consensus sequence could be identified even in other, non-sialidase proteins, indicating a common function or the evolutionary relatedness of these proteins. |
| Databáze: | OpenAIRE |
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