Anti-stress activity of Propionibacterium freudenreichii : identification of a reactivative protein

• Published in: Antonie van Leeuwenhoek 2004-01, Vol.85 (1), p.53-62
• Main Authors: Vorobjeva, Lena, Leverrier, Pauline, Zinchenko, Aleksei, Boyaval, Patrick, Khodjaev, Evgeni, Varioukhina, Svetlana, Ponomareva, Galina, Gordeeva, Elena, Jan, Gwénaël
• Format: Article
• Language: English
• Subjects: 4-Nitroquinoline-1-oxide - pharmacology; Aminacrine - pharmacology; Amino Acid Sequence; Ammonium; Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - drug effects; Bacterial Proteins - genetics; Bacterial Proteins - isolation & purification; Bile Acids and Salts - pharmacology; Carcinogens - pharmacology; Cysteine Synthase - chemistry; Cysteine Synthase - genetics; Cysteine Synthase - isolation & purification; DNA Damage; DNA Repair - drug effects; DNA Repair - radiation effects; E coli; Escherichia coli; Escherichia coli - drug effects; Escherichia coli - genetics; Escherichia coli - physiology; Escherichia coli - radiation effects; Gene Expression Regulation, Bacterial - drug effects; Hydrogen Peroxide - pharmacology; Mass Spectrometry; Methylnitronitrosoguanidine - pharmacology; Molecular Sequence Data; Mutagenesis; Oxidative stress; Peptide Fragments - chemistry; Propionibacterium - drug effects; Propionibacterium - genetics; Propionibacterium - physiology; Propionibacterium - radiation effects; Propionibacterium freudenreichii; Proteins; Salmonella typhimurium; Sequence Alignment; Sequence Homology, Amino Acid; Ultraviolet radiation; Ultraviolet Rays
• ISSN: 0003-6072; 1572-9699
• DOI: 10.1023/B:ANTO.0000020276.18127.99

Propionibacterium freudenreichii subsp. shermanii is known to prevent mutations caused by various agents such as N-methyl-N'-nitro-N-nitrosoguanidine, 9-aminoacridine, 4-nitro-quinoline-1-oxide and by UV radiation in both prokaryotic and eukaryotic cells. It was also shown to prevent or repair damage caused by H(2)O(2) or UV radiation in Salmonella typhimurium and Escherichia coli, a characteristic previously designated as reactivative effect. In order to characterise this effect at the molecular level, we have purified the active component from a P. freudenreichii cell-free extract using a combination of ammonium sulfate precipitation, anion-exchange and size-exclusion chromatography. The isolated 35 kDa protein was then identified using both N-terminal and internal peptide sequencing as a cysteine synthase. The latter was localised in the P. freudenreichii proteomic map. It is constitutively expressed but also clearly induced during adaptation to detergent and heat, but not acid, stresses. The biological meaning of cysteine synthase in the context of adaptation to oxidative and non-oxidative stresses is discussed.