Nucleotide Sequence of a Pectate Lyase Structural Gene, pel1 of Erwinia carotovora subsp. carotovora Strain 71 and Structural Relationship of pel1 with Other pel Genes of Erwinia Species. Asita Chatterjee. Department of Plant Pathology, 108 Waters Hall, University of Missouri-Columbia, Columbia, MO 65211 U.S.A. Yang Liu, and Arun K. Chatterjee. Department of Plant Pathology, 108 Waters Hall, University of Missouri-Columbia, Columbia, MO 65211 U.S.A. MPMI 8:92-95. Accepted 12 September 1994. Copyright 1995 The American Phytopathological Society.

Of the various exoproteins secreted by Erwinia carotovora subsp. carotovora strain 71, Pell is the major pcclate lyase species with tissue macerating activity. Nucleolide sequencing of a 2.2-kb pell+ DNA segment revealed a 1,122 base pair open reading frame which could encode pre-Pell of 374 amino acid residues. A signal peptide of 22 amino acid residues is present within the NH2-terminaI region of pre-Pell. Transcription of pell was initiated at the guanine residue 111 base pairs upstream of the start codon. Consensus sequences for Ihe binding of KdgR, a negative regulatory factor known to control some of the E. chrysanlhemi pectinases, Hank the promoter of pell. Although pell belongs to the pelBC family, it is more closely related to the pel genes of E. carotovora than to the pelBC genes of E. chrysanthemi