AepA of Pectobacterium is not involved in the regulation of extracellular plant cell wall degrading enzymes production

• Published in: Molecular genetics and genomics : MGG 2010-06, Vol.283 (6), p.541-549
• Main Authors: Kõiv, Viia, Andresen, Liis, Mäe, Andres
• Format: Article
• Language: English
• Subjects: Amidohydrolases; Amidohydrolases - genetics; Amidohydrolases - metabolism; Amidohydrolases - physiology; Animal Genetics and Genomics; Bacteria; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - physiology; Biochemistry; Biomedical and Life Sciences; Cell Wall - metabolism; Cloning; Cloning, Molecular; Enzymes; Enzymes - biosynthesis; Enzymes - genetics; Enzymes - metabolism; Enzymes - physiology; Extracellular Space - metabolism; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Genes; Genes, Bacterial; Genomics; Glycerol; Human Genetics; Life Sciences; Microbial Genetics and Genomics; Original Paper; PCWDE; Pectobacterium - enzymology; Pectobacterium - genetics; Pectobacterium - pathogenicity; Plant Genetics and Genomics; plant pathogenic bacteria; Plants - chemistry; Plants - microbiology; Plants - ultrastructure; Plasmids; Potatoes; Regulation; Solanum tuberosum - microbiology; substrate specificity; Transfection; Vectors (Biology); Virulence; Virulence Factors - genetics; Virulence Factors - metabolism; Virulence Factors - physiology
• ISSN: 1617-4615; 1617-4623
• DOI: 10.1007/s00438-010-0540-9

Plant cell wall degrading enzymes (PCWDE) are the major virulence determinants in phytopathogenic Pectobacterium, and their production is controlled by many regulatory factors. In this study, we focus on the role of the AepA protein, which was previously described to be a global regulator of PCWDE production in Pectobacterium carotovorum (Murata et al. in Mol Plant Microbe Interact 4:239-246, 1991). Our results show that neither inactivation nor overexpression of aepA affects PCWDE production in either Pectobacterium atrosepticum SCRI1043 or Pectobacterium carotovorum subsp. carotovorum SCC3193. The previously published observation based on the overexpression of aepA could be explained by the presence of the adjacent regulatory rsmB gene in the constructs used. Our database searches indicated that AepA belongs to the YtcJ subfamily of amidohydrolases. YtcJ-like amidohydrolases are present in bacteria, archaea, plants and some fungi. Although AepA has 28% identity with the formamide deformylase NfdA in Arthrobacter pascens F164, AepA was unable to catalyze the degradation of NdfA-specific N-substituted formamides. We conclude that AepA is a putative aminohydrolase not involved in regulation of PCWDE production.