A polygalacturonase of animal origin isolated from the root-knot nematode Meloidogyne incognita

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...

Full description

Saved in:
Bibliographic Details
Published inFEBS letters Vol. 522; no. 1; pp. 109 - 112
Main Authors Jaubert, Stéphanie, Laffaire, Jean-Baptiste, Abad, Pierre, Rosso, Marie-Noëlle
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 03.07.2002
Wiley
Subjects
Animals
Base Sequence
Cellular Biology
Escherichia coli
Gene Expression
Genetic Vectors
Life Sciences
Molecular Sequence Data
Nematode
Pectin
Phylogeny
Plant Roots - parasitology
Polygalacturonase
Polygalacturonase - classification
Polygalacturonase - genetics
Polygalacturonase - isolation & purification
Stylet secretion
Tylenchoidea - enzymology
Tylenchoidea - genetics
PG, polygalacturonase
J2s, second stage juveniles
Stylet secretion
Nematode
Pectin
Polygalacturonase
cds, coding sequence
PGA, polygalacturonic acid
EST, expressed sequence tag
RELATION HOTE PARASITE
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)02906-X