Abstract
By site-specific mutagenesis, the hydrophobic conserved amino acids and the C-terminal GG doublet of the leader peptide of pre-mesentericin Y105 were demonstrated to be critical for optimal secretion of mesentericin Y105, as well as for the maturation of the pre-bacteriocin by the protease portion of the ABC transporter MesD.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Bacteriocins / chemistry
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Bacteriocins / genetics*
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Bacteriocins / metabolism*
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Cytoplasm / metabolism
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Hydrophobic and Hydrophilic Interactions
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Leuconostoc / genetics*
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Leuconostoc / metabolism*
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Protein Structure, Tertiary
Substances
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Bacteriocins
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mesentericin Y105 protein, Leuconostoc mesenteroides