Effect of signal sequence alterations on export of levansucrase in Bacillus subtilis.
A series of alterations in the Bacillus amyloliquefaciens levansucrase signal peptide were made by in vitro mutagenesis, and their effect on the secretion of levansucrase in Bacillus subtilis was studied. Some of the alterations resulted in a completely defective signal peptide. These included the removal of positively charged residues from the N-terminus and disruption of the hydrophobic core of the signal peptide either by introducing a charged residue or by deleting five or more amino acids. Analysis of the signal peptide processing-site alterations revealed that small residues are preferred at the -1 and -3 positions. However, a wide variety of amino acids are tolerated at the +1 position.
Borchert
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Central Research and Development Division, E. I. du Pont de Nemours Inc., Wilmington, Delaware 19880-0228.
Nagarajan
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D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D006602:Hexosyltransferases / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D015345:Oligonucleotide Probes; D011487:Protein Conformation; D021382:Protein Sorting Signals / Q000235:genetics*
D015345:Oligonucleotide Probes; D021382:Protein Sorting Signals; D006602:Hexosyltransferases; C021513:levansucrase