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. 1989 Jul;171(7):3767–3774. doi: 10.1128/jb.171.7.3767-3774.1989

Excretion of the egl gene product of Pseudomonas solanacearum.

J Z Huang 1, M Sukordhaman 1, M A Schell 1
PMCID: PMC210123  PMID: 2738021

Abstract

Pseudomonas solanacearum is an important phytopathogen which excretes a variety of extracellular enzymes. Pulse-chase experiments showed that one of these enzymes, a beta-1,4-endoglucanase (EGL) encoded by the egl gene, is synthesized as a higher-molecular-weight precursor polypeptide (pEGL) which is subsequently excreted into the extracellular medium as a 43-kilodalton mature protein. S1 nuclease transcript mapping and DNA sequence analysis were used to identify the transcription start site and the possible translation start site of egl. Pulse-chase experiments and comparison of the putative NH2-terminal amino acid sequence of pEGL with the actual NH2-terminal amino acid sequence of mature excreted EGL suggested that pEGL has a 45-residue leader sequence preceding the N terminus of EGL which is proteolytically cleaved during export to the extracellular environment. The first 20 residues of the leader sequence resembled a typical lipoprotein signal peptide. The excretion of EGL by P. solanacearum apparently requires a membrane potential since it was blocked by carbonyl cyanide m-chlorophenyl hydrazone.

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