Search engine for discovering works of Art, research articles, and books related to Art and Culture
ShareThis
Javascript must be enabled to continue!

Identification and characterization of a peptidoglycan hydrolase from Rhodobacter johrii

View through CrossRef
Abstract The bacterial whole genome sequences are available in the database therefore explored for the varieties of known and unknown proteins. Bacteria harbor various peptidoglycan hydrolases that cleave peptidoglycan and play an important role in the cell division, growth, spore differentiation and development. In the present study, we report a peptidoglycan hydrolase in an endospore producing phototrophic proteobacterium Rhodobacter johrii. The Peptidoglycan Hydrolase of Rba. johrii (PgHR) can actively hydrolyze the intact spore cortex peptidoglycan (sacculi). The protein contains a pre-peptide precursor which has a Hydrolase-2 (PF07486) family conserved domain. PgHR protein has SleB like properties which are spore cortex-lytic enzymes involved in the depolymerization of cortex peptidoglycan present and characterized in Bacillus spp. The expression pattern of PgHR through qRT-PCR suggests its role in stationary phase of Rba. johrii. This is a new type of peptidoglycan hydrolase reported from a proteobacterium.
Springer Science and Business Media LLC
Title: Identification and characterization of a peptidoglycan hydrolase from Rhodobacter johrii
Description:
Abstract The bacterial whole genome sequences are available in the database therefore explored for the varieties of known and unknown proteins.
Bacteria harbor various peptidoglycan hydrolases that cleave peptidoglycan and play an important role in the cell division, growth, spore differentiation and development.
In the present study, we report a peptidoglycan hydrolase in an endospore producing phototrophic proteobacterium Rhodobacter johrii.
The Peptidoglycan Hydrolase of Rba.
johrii (PgHR) can actively hydrolyze the intact spore cortex peptidoglycan (sacculi).
The protein contains a pre-peptide precursor which has a Hydrolase-2 (PF07486) family conserved domain.
PgHR protein has SleB like properties which are spore cortex-lytic enzymes involved in the depolymerization of cortex peptidoglycan present and characterized in Bacillus spp.
The expression pattern of PgHR through qRT-PCR suggests its role in stationary phase of Rba.
johrii.
This is a new type of peptidoglycan hydrolase reported from a proteobacterium.

Related Results

Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity
Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity
Aminopeptidase B (Ap B; EC 3.4.11.6) is a zinc-binding protein that contains the consensus sequence HEXXHX18E (324-347), conserved among the M1 family of metallopeptidases. To dete...
Peptidoglycan synthesis in Tannerella forsythia: Scavenging is the modus operandi
Peptidoglycan synthesis in Tannerella forsythia: Scavenging is the modus operandi
SummaryTannerella forsythia is a Gram‐negative oral pathogen strongly associated with periodontitis. This bacterium has an absolute requirement for exogenous N‐acetylmuramic acid (...
Systematic genome-guided discovery of antagonistic interactions between archaea and bacteria
Systematic genome-guided discovery of antagonistic interactions between archaea and bacteria
ABSTRACTThe social life of archaea is poorly understood. In particular, even though competition and conflict are common themes in microbial communities, there is scant evidence doc...
Two-step localization driven by peptidoglycan hydrolase in interbacterial predation
Two-step localization driven by peptidoglycan hydrolase in interbacterial predation
Abstract Mechanisms of bacterial predation are crucial for revealing microbial adaptation strategies and interaction behaviors in the environment, yet they remain po...
Mechanism of lateral cell-wall expansion at a constant diameter in Bacillus subtilis
Mechanism of lateral cell-wall expansion at a constant diameter in Bacillus subtilis
Abstract In Escherichia coli, lateral cell-wall expansion during growth occurs by cross-linking of new glycan strands to the existing peptidoglycan network. However, it i...
A GMR enzymatic assay for quantifying nuclease and peptidase activity
A GMR enzymatic assay for quantifying nuclease and peptidase activity
Hydrolytic enzymes play crucial roles in cellular processes, and dysregulation of their activities is implicated in various physiological and pathological conditions. These enzymes...
De-identifying government datasets:
De-identifying government datasets:
De-identification is a general term for any process of removing the association between a set of identifying data and the data subject. This document describes the use of de-identi...

Back to Top