Cloning and characterization of a prolinase gene (pepR) from Lactobacillus rhamnosus.

ABSTRACT: A peptidase gene expressing L-proline-beta-naphthylamide-hydrolyzing activity was cloned from a gene library of Lactobacillus rhamnosus 1/6 isolated from cheese. Peptidase-expressing activity was localized in a 1.5-kb SacI fragment. A sequence analysis of the SacI fragment revealed the presence of one complete open reading frame (ORF1) that was 903 nucleotides long. The ORF1-encoded 34.2-kDa protein exhibited 68% identity with the PepR protein from Lactobacillus helveticus. Additional sequencing revealed the presence of another open reading frame (ORF2) following pepR; this open reading frame was 459 bp long. Northern (RNA) and primer extension analyses indicated that pepR is expressed both as a monocistronic transcriptional unit and as a dicistronic transcriptional unit with ORF2. Gene re

SUBMITTER: Varmanen P 

PROVIDER: S-EPMC106238 | biostudies-literature | 1998 May

REPOSITORIES: biostudies-literature