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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

Alfano, J.R.; Ham, J.H.; Collmer, A.

Journal of Bacteriology 177(15): 4553-4556

1995


ISSN/ISBN: 0021-9193
PMID: 7635842
Accession: 003005625

Erwinia chrysanthemi mutant CUCPB5047, delta (pellA pelE) delta (pelB pelC)::28bp delta (pelX) delta 4bp pehX::omega Cmr, was constructed, mutated with Tn5tac1, and screened for isopropyl-beta-D thiogalactopyranoside-dependent pectate lyase (Pel) production. A Kmr 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.

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