Cloning, characterization and phenotypic expression in Escherichia coli of catF, which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae

Applied Microbiology and Biotechnology
M G KlotzA J Anderson

Abstract

The phytophathogenic, gram-negative bacterium Pseudomonas syringae pv. syringae 61 contains three isozymes of catalase (EC 1.11.1.6), which have been proposed to play a role in the bacterium's responses to various environmental stresses. To study the role of individual isozymes, the gene coding for the catalytic subunit of one catalase isozyme was cloned from a cosmid library hosted in Escherichia coli DH5 alpha by using a designed catalase-specific DNA probe for the screening. One out of four clones with a catalase-positive genotype was subcloned and a pUC19-based 2.7 x 10(3)-base (2.7-kb) insert subclone, pMK3E5, was used to transform catalase-deficient E. coli strain UM255 (HPI-, HPII-). The transformants contained a single isozyme of catalase that had electrophoretic and enzymic properties similar to catalase isozyme CatF from P. syringae pv. syringae 61. Analysis of the sequenced 2.7-kb insert DNA revealed six putative open-reading frames (ORF). The 1542-base-pair DNA sequence of ORF2, called catF, encodes a peptide of 513 amino acid residues with a calculated molecular mass of 66.6 kDa. The amino acid sequence deduced from catF had homology to the primary structure of true catalases from mammals, plants, yeasts and bacter...Continue Reading

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Citations

Sep 12, 2006·Eukaryotic Cell·Steven S GilesJohn R Perfect
Feb 15, 2011·Journal of Bioscience and Bioengineering·Haruhiko YamaguchiToru Nakayama
Oct 31, 2013·Scientific Reports·Tadayuki IwaseYoshimitsu Mizunoe
Mar 21, 2007·FEMS Immunology and Medical Microbiology·Panagoula CharalabousJohn W Smalley
Nov 19, 2011·FEMS Microbiology Letters·Helen Fones, Gail M Preston

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