Premium
Molecular cloning and nucleotide sequence of the pectin methyl esterase gene of Erwinia chrysanthemi B374
Author(s) -
Plastow G. S.
Publication year - 1988
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1988.tb00026.x
Subject(s) - biology , gene , esterase , nucleic acid sequence , genetics , molecular cloning , cloning (programming) , sequence (biology) , peptide sequence , biochemistry , enzyme , computer science , programming language
Summary The gene encoding pectin methyl esterase ( pme ) has been cloned from Erwinia chrysanthemi B374. Expression of pme in Escherichia coli allowed the enzyme to be characterized. Pectin methyl esterase (PME) was found to have an apparent molecular weight of 36000 Daltons and an isoelectric point of approximately 9.9. The structural gene was sequenced and consists of a 1098‐bp open reading frame encoding a polypeptide of 39318 Daltons, which includes an amino‐terminal signal peptide. The isolation of the Erwinia gene provides a simple method for the production of PME free from depolymerizing pectinases thereby extending its potential uses.