Influence of amino acid substitutions in the leader peptide on maturation and secretion of mesentericin Y105 by Leuconostoc mesenteroides.
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.
Aucher
Willy
W
Institut de Biologie Moléculaire et d'Ingénierie Génétique, Equipe de Microbiologie Fondamentale et Appliquée, UMR CNRS 6008, Université de Poitiers, Poitiers, France.
Lacombe
Christian
C
Héquet
Arnaud
A
Frère
Jacques
J
Berjeaud
Jean-Marc
JM
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001430:Bacteriocins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D007934:Leuconostoc / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017434:Protein Structure, Tertiary
D001430:Bacteriocins; C079275:mesentericin Y105 protein, Leuconostoc mesenteroides
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