Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine- rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes

J. R. Alfano, Hyun Ham Jong Hyun Ham, A. Collmer

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Erwinia chrysanthemi mutant CUCPB5047, Δ(pelA pelE) Δ(pelB pelC)::28bp Δ(pelX) Δ4bp pehX::ΩCm(r), was constructed, mutated with Tn5tac1, and screened for isopropyl-β-D-thiogalactopyranoside-dependent pectate lyase (Pel) production. AKm(r) SacI fragment from the hyperexpressing Pel+ mutant CUCPB5066 was cloned into Escherichia coli and sequenced. The gene identified, pelL, encodes a novel, asparagine-rich, highly alkaline enzyme that is similar in primary structure to PelX and in enzymological properties to PelE.

Original languageEnglish (US)
Pages (from-to)4553-4556
Number of pages4
JournalJournal of bacteriology
Volume177
Issue number15
DOIs
StatePublished - 1995

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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