Genomic analysis of Caballeronia sp. DA-9 reveals its role in glutathione metabolism.

Glutathione (GSH) is a well-known tripeptide composed of glutamic acid, cysteine and glycine. It plays critical roles in maintaining the redox homeostasis of cells and in cell cycle regulation, apoptosis, immunological defense, and pathological abnormalities. Caballeronia sp. DA-9, a Gram-negative and aerobic bacterium, was isolated from the sediment collected from the Weddell Sea. Here, we report the complete genome sequence of strain DA-9 and its genomic characteristics to synthesize and catabolize GSH. The genome of strain DA-9 contains three circular chromosomes and two plasmids. Genomic analysis showed that strain DA-9 contained a set of genes involved in GSH metabolism, indicating that it possesses the potential ability to synthesize and catabolize GSH. This study provides novel insights into GSH metabolism by marine microorganisms.

• Publication year

  2025

• Venue

  Marine Genomics

• Publication date

  2025-09-01

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1016/j.margen.2025.101214PMID 41344780
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• An Update on Glutathione's Biosynthesis, Metabolism, Functions, and Medicinal Purposes.

  2023cited by this paper
• Discovery of a widespread prokaryotic 5-oxoprolinase that was hiding in plain sight

  2017cited by this paper
• Microbial production of glutathione

  2017cited by this paper
• Oxidative‐stress detoxification and signalling in cyanobacteria: the crucial glutathione synthesis pathway supports the production of ergothioneine and ophthalmate

  2016cited by this paper
• Cellular functions of glutathione.

  2013cited by this paper
• Glutathione synthesis.

  2013cited by this paper
• Redox-dependent stability of the γ-glutamylcysteine synthetase enzyme of Escherichia coli: a novel means of redox regulation.

  2013cited by this paper
• DNAPlotter: circular and linear interactive genome visualization

  2008cited by this paper
• RNAmmer: consistent and rapid annotation of ribosomal RNA genes

  2007cited by this paper
• KAAS: an automatic genome annotation and pathway reconstruction server

  2007cited by this paper
• Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis.

  2004cited by this paper
• Cellular glutathione and thiols metabolism.

  2002cited by this paper
• The 5' terminal oligopyrimidine tract confers translational control on TOP mRNAs in a cell type- and sequence context-dependent manner.

  1997cited by this paper
• xerB, an Escherichia coli gene required for plasmid ColE1 site‐specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase.

  1989cited by this paper
• On the discovery of glutathione.

  1988cited by this paper
• The nucleotide sequence of the gene for gamma-glutamylcysteine synthetase of Escherichia coli.

  1986cited by this paper
• The nudeotide sequence of the gene for γ-glutamylcysteine synthetase of Escherichia coli

  1986cited by this paper
• Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II.

  1984cited by this paper
• Glutathione.

  1983cited by this paper
• Occurrence of glutathione in bacteria

  1978cited by this paper
• Mapping of gshA, a gene for the biosynthesis of glutathione in Eschericha coli K12

  1975cited by this paper

• No citing papers are available for this paper.