1995
DOI: 10.1111/j.1365-2958.1995.tb02295.x
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A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export

Abstract: Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double-glycine-type leader peptides are unrelated to the N-terminal signal sequences w… Show more

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Cited by 546 publications
(554 citation statements)
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“…Analogous to similar studies on the protease domain of bifunctional transporters for nonlantibiotic bacteriocins (24)(25)(26), expression in E. coli of the first 150 residues of LctT resulted in an active protease that correctly hydrolyzed the amide bond between Ala-1 and Lys1 in LctA. These findings indicate that the transmembrane transporter domain of LctT is not required for substrate recognition and proteolysis.…”
Section: Discussionmentioning
confidence: 60%
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“…Analogous to similar studies on the protease domain of bifunctional transporters for nonlantibiotic bacteriocins (24)(25)(26), expression in E. coli of the first 150 residues of LctT resulted in an active protease that correctly hydrolyzed the amide bond between Ala-1 and Lys1 in LctA. These findings indicate that the transmembrane transporter domain of LctT is not required for substrate recognition and proteolysis.…”
Section: Discussionmentioning
confidence: 60%
“…Three conserved residues of LctT proposed to be involved in peptide bond cleavage (Cys12, His90, and Asp106) (24) were mutated to investigate their importance in amide bond hydrolysis. The involvement of these residues in catalysis has been suggested, but never experimentally tested for lantibiotic proteases.…”
Section: Proteolytic Activity Of His 10 -Lctt150 Mutant Proteinsmentioning
confidence: 99%
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“…The residual activity of this intracellular bacteriocin precursor, although low, may necessitate the observed co-expression of immunity protein in wild type C. piscicola that is encoded on the same operon. 3 Reduction of antimicrobial properties for precursors of other types of bacteriocins has previously been suggested (20).…”
Section: Discussionmentioning
confidence: 99%
“…The ABC transporters for production of class IIa bacteriocins have an extra N-terminal cysteine protease domain that is used to cut off the leader after the GG-motif (Figure 3, p30) (Havarstein et al 1995). The GG-leader is consequently removed by the ABC transporters during transmembrane translocation, and the mature bacteriocin is subsequently secreted (Havarstein et al 1995). By exchanging the leader peptides, it is possible to heterologously express class IIa bacteriocin via another secretion system, which may be more efficient (Ennahar et al 2000).…”
Section: Biosynthesismentioning
confidence: 99%