Pseudomonas aeruginosa LasD processes the inactive LasA precursor to the active protease form
Related Experiment Video
Updated: Sep 17, 2026

Replication of the Ordered, Nonredundant Library of Pseudomonas aeruginosa strain PA14 Transposon Insertion Mutants
Published on: May 4, 2018
1Department of Microbiology, Ohio State University, Columbus, Ohio 43210-1292, USA.
Abstract:
LasA and LasD are staphylolytic proteinases which are secreted by the opportunistic pathogen Pseudomonas aeruginosa. We have previously described the purification and characterization of both LasA and LasD, a 21-kDa protein which shares many of the enzymatic properties of LasA. In this follow-up study we describe the isolation of the 42-kDa precursor of LasA (proLasA) and demonstrate the ability of the purified LasD proteinase to cleave the inactive proLasA to the 20-kDa active form of the proteinase.
More Related Videos
09:12Live Cell Analysis of Shear Stress on Pseudomonas aeruginosa Using an Automated Higher-Throughput Microfluidic System
Published on: January 16, 2019
08:34Generation of In-Frame Gene Deletion Mutants in Pseudomonas aeruginosa and Testing for Virulence Attenuation in a Simple Mouse Model of Infection
Published on: January 8, 2020
Related Concept Videos
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Caspases
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome Structure
The proteasome is an...
Gene Regulation in Microbial Communities: Quorum Sensing
Clinical Significance of Antibiotic Resistance