Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the α-amylase gene from Bacillus amyloliquefaciens

Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium

“…In addition there is also a peptide extension beyond the hydrophobic core segment (residues 29 -34) which other than in all other known bacterial systems separates the hydrophobic segment from the processing site. Similar features have very recently also been noticed in the signal sequence of the a-amylase from B. amyloliquefaciens, another secretory protein from the genus aacillus (34). It seems therefore likely that these structural variations reflect modifications of the mechanism used for the secretion of proteins in Gram-positive or in Gram-negative bacteria: Firstly, the long, highly charged NH2-terminus (see Fig.…”

Synthesis of OmpA Protein of Escherichia coli K12 in Bacillus subtilis

“…The quantity of the released phenylthiohydantoin amino acids also corresponded to the amount of the degraded protein. The sequence obtained was identical to the N-terminal sequence of the a-amylase signal peptide deduced from the DNA sequence (Palva et al, 1981). The result shows that the signal peptide was not cleaved when OmpA228 was synthesized in B. subtilis from the plasmid pKTH158.…”

“…Plasmids were isolated on a large scale from E. coli as described by Clewell & Helinski (1969) and from B. subtilis as described by Palva et al (1981). Some batches were further purified in a neutral sucrose gradient (Palva et al, 1981).…”

Molecular cloning, overexpression and characterization of the raw-starch-digesting α-amylase of Bacillus amyloliquefaciens

“…Previously, the molecular weight of the α-amylase from B. amyloliquefaciens has been estimated to be between 40-60 kDa as determined by SDS-PAGE, sedimentation properties, gel filtration, amino acid composition analysis and cyanogen bromide fragment analysis (Detera & Friedberg 1979;Chung & Friedberg 1980;Palva et al 1981). In the present case the overexpressed enzyme was purified and the molecular weight was determined to be 58 kDa.…”