A genetic insight into peptide and amino-acid utilization by Propionibacterium freudenreichii LMG 16415.
In this note the genetic characterization of the peptide degrading system of Propionibacterium freudenreichii was addressed. Genomic fragments of P. freudenreichii subsp. freudenreichii LMG 16415 were cloned in Escherichia coli XL1 Blue, and those leading to an increase in peptidase-like activity using chromogenic substrates aminoacyl-beta-naphtylamides (aminoacyl-betaNA) were isolated and sequenced. This strategy allowed the identification of partial gene regions of P. freudenreichii LMG 16415 with significant similarity to proteins directly or indirectly involved in peptide and amino acid metabolism, i.e., an oligopeptide transporter, a D-amino acid oxidase, a muropeptidase, and an ABC transporter involved in osmoregulation similar to glycine betaine transporters.
Rossi
Franca
F
Dipartimento Scientifico e Tecnologico, Università degli Studi di Verona, Strada Le Grazie 15, 37134, Verona, Italy.
Gatto
Veronica
V
Marzotto
Marta
M
Torriani
Sandra
S
D000596:Amino Acids / Q000378:metabolism*; D002863:Chromogenic Compounds; D004926:Escherichia coli / Q000235:genetics; D005189:False Positive Reactions; D016366:Open Reading Frames / Q000235:genetics; D010447:Peptide Hydrolases / Q000235:genetics*; D010455:Peptides / Q000378:metabolism*; D011423:Propionibacteriaceae / Q000235:genetics* / Q000378:metabolism; D017422:Sequence Analysis, DNA / Q000379:methods*
D000596:Amino Acids; D002863:Chromogenic Compounds; D010455:Peptides; D010447:Peptide Hydrolases