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A polygalacturonase of animal origin isolated from the root‐knot nematode Meloidogyne incognita 1
Author(s) -
Jaubert Stéphanie,
Laffaire Jean-Baptiste,
Abad Pierre,
Rosso Marie-Noëlle
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02906-x
Subject(s) - meloidogyne incognita , terra incognita , biology , pectinase , root knot nematode , complementary dna , nematode , heterologous , signal peptide , meloidogyne javanica , heterologous expression , microbiology and biotechnology , escherichia coli , gene , enzyme , peptide sequence , biochemistry , recombinant dna , ecology
The first animal polygalacturonase (PG, EC 2.1.15) encoding cDNA, Mi‐pg‐1 , was cloned from the plant parasitic nematode Meloidogyne incognita . The enzymatic activity of MI‐PG‐1 was confirmed after heterologous expression in Escherichia coli . The presence of a predicted signal peptide on the MI‐PG‐1 sequence together with the specific localization of the transcripts of the Mi‐pg‐1 gene in the oesophageal glands of infective juveniles imply that MI‐PG‐1 could be secreted into plant tissues. The potential role of MI‐PG‐1 in parasitism is discussed.