Maturation by LctT Is Required for Biosynthesis of Full-Length Lantibiotic Lacticin 481
نویسندگان
چکیده
منابع مشابه
Maturation by LctT is required for biosynthesis of full-length lantibiotic lacticin 481.
In lantibiotic lacticin 481 biosynthesis, LctT cleaves the precursor peptide and exports mature lantibiotic. Matrix-assisted laser desorption ionization-time of flight mass spectrometry revealed that a truncated form of lacticin 481 is produced in the absence of LctT or after cleavage site inactivation. Production of truncated lacticin 481 is 4-fold less efficient, and its specific activity is ...
متن کاملLacticin 481: in vitro reconstitution of lantibiotic synthetase activity.
The lantibiotic lacticin 481 is synthesized on ribosomes as a prepeptide (LctA) and posttranslationally modified to its mature form. These modifications include dehydration of serines and threonines, followed by intramolecular addition of cysteines to the unsaturated amino acids, which generates cyclic thioethers. This process breaks eight chemical bonds and forms six newbonds and is catalyzed ...
متن کاملIn vitro reconstitution and substrate specificity of a lantibiotic protease.
Lacticin 481 is a lanthionine-containing bacteriocin (lantibiotic) produced by Lactococcus lactis subsp. lactis. The final steps of lacticin 481 biosynthesis are proteolytic removal of an N-terminal leader sequence from the prepeptide LctA and export of the mature lantibiotic. Both proteolysis and secretion are performed by the dedicated ATP-binding cassette (ABC) transporter LctT. LctT belongs...
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Lantibiotics are a family of antibacterial peptide natural products characterized by the post-translational installation of the thioether-containing amino acids lanthionine and methyllanthionine. Until recently, only a single naturally occurring stereochemical configuration for each of these cross-links was known. The discovery of lantibiotics with alternative lanthionine and methyllanthionine ...
متن کاملLacticin 481 Synthetase as a General Serine/Threonine Kinase
Methods that introduce posttranslational modifications in a general, mild, and non-sequence-specific manner using biologically produced peptides have great utility for investigation of the functions of these modifications. In this study, the substrate promiscuity of a lantibiotic synthetase was exploited for the preparation of phosphopeptides, glycopeptides, and peptides containing analogs of m...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2005
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.71.1.562-565.2005