Characterization of the Agrobacterium vitis pehA gene and comparison of the encoded polygalacturonase with the homologous enzymes from Erwinia carotovora and Ralstonia solanacearum.
DNA sequencing of the Agrobacterium vitis pehA gene revealed a predicted protein with an M(r) of 58,000 and significant similarity to the polygalacturonases of two other plant pathogens, Erwinia carotovora and Ralstonia (= Pseudomonas or Burkholderia) solanacearum. Sequencing of the N terminus of the PehA protein demonstrated cleavage of a 34-amino-acid signal peptide from pre-PehA. Mature PehA accumulated primarily in the periplasm of A. vitis and pehA+ Escherichia coli cells during exponential growth. A. vitis PehA released dimers, trimers, and monomers from polygalacturonic acid and caused less electrolyte leakage from potato tuber tissue than did the E. carotovora and R. solanacearum polygalacturonases.
Herlache
T C
TC
Department of Plant Pathology, Cornell University, Ithaca, New York 14853, USA.
Hotchkiss
A T
AT
Burr
T J
TJ
Collmer
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D019117:Burkholderia / Q000201:enzymology / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D005798:Genes, Bacterial; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D016973:Pectobacterium carotovorum / Q000201:enzymology / Q000235:genetics; D010944:Plants / Q000382:microbiology; D011096:Polygalacturonase / Q000235:genetics*; D012231:Rhizobium / Q000201:enzymology* / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013347:Subcellular Fractions / Q000201:enzymology
D004269:DNA, Bacterial; D011096:Polygalacturonase