TY - JOUR
T1 - Biochemical and phylogenetic analysis of CEBiP-like LysM domain-containing extracellular proteins in higher plants
AU - Fliegmann, Judith
AU - Uhlenbroich, Sandra
AU - Shinya, Tomonori
AU - Martinez, Yves
AU - Lefebvre, Benoit
AU - Shibuya, Naoto
AU - Bono, Jean Jacques
N1 - Funding Information:
We would like to thank Dr. C. Gough for the EST clones, Dr. H. Berglund for providing the pTH19 cloning vector, Dr. P. Ratet for the plasmid pPR97, Dr. M. Boutry for the anti-H + -ATPase antiserum, Dr. G. Borderies for continuous support, C. Arlot for the purification of MtLYM1, Y. Sekiguchi for contributing to BY-2 transformation and binding assays, and Drs. J. Cullimore, H. Kaku, A. Jauneau, and T. Kroj for helpful discussion. This work was funded in parts by the Région Midi-Pyrénées and the CNRS (PhD grant to SU), the French Agence Nationale de la Recherche (contracts ANR-08-BLAN-0208-01 “Sympasignal” and ANR-05-BLAN-0243-01 “NodBindsLysM”), and by the European Community’s Sixth Framework Program through a Marie Curie Research Training Network (contract MRTN-CT-2006-035546 “Nodperception”).
PY - 2011/7
Y1 - 2011/7
N2 - The chitin elicitor-binding protein (CEBiP) from rice was the first plant lysin motif (LysM) protein for which the biological and biochemical function had been established. It belongs to a plant-specific family of extracellular LysM proteins (LYMs) for which we analyzed the phylogeny. LYMs are present in vascular plants only, where an early gene duplication event might have resulted in two types which were retained in present day genomes. LYMs consist of a signal peptide, three consecutive LysMs, separated by cysteine pairs, and a C-terminal region without any known signature, whose length allows the distinction between the two types, and which may be followed by a glycosylphosphatidylinositol (GPI) anchor motif. We analyzed a representative of each type, MtLYM1 and MtLYM2, from Medicago truncatula at the biochemical level and with respect to their expression patterns and observed some similarities but also marked differences. MtLYM1 and MtLYM2 proved to be very different with regard to abundance and apparent molecular mass on SDS-PAGE. Both undergo several post-translational modifications, including N-glycosylation and the addition of a GPI anchor, which would position the proteins at the outer face of the plasma membrane. Only MtLYM2, but not MtLYM1, showed specific binding to biotinylated N-acetylchitooctaose in a manner similar to CEBiP, which belongs to the same type. We postulate that LYM2-type proteins likely function in the perception of chitin-related molecules, whereas possible functions of LYM1-type proteins remain to be elucidated.
AB - The chitin elicitor-binding protein (CEBiP) from rice was the first plant lysin motif (LysM) protein for which the biological and biochemical function had been established. It belongs to a plant-specific family of extracellular LysM proteins (LYMs) for which we analyzed the phylogeny. LYMs are present in vascular plants only, where an early gene duplication event might have resulted in two types which were retained in present day genomes. LYMs consist of a signal peptide, three consecutive LysMs, separated by cysteine pairs, and a C-terminal region without any known signature, whose length allows the distinction between the two types, and which may be followed by a glycosylphosphatidylinositol (GPI) anchor motif. We analyzed a representative of each type, MtLYM1 and MtLYM2, from Medicago truncatula at the biochemical level and with respect to their expression patterns and observed some similarities but also marked differences. MtLYM1 and MtLYM2 proved to be very different with regard to abundance and apparent molecular mass on SDS-PAGE. Both undergo several post-translational modifications, including N-glycosylation and the addition of a GPI anchor, which would position the proteins at the outer face of the plasma membrane. Only MtLYM2, but not MtLYM1, showed specific binding to biotinylated N-acetylchitooctaose in a manner similar to CEBiP, which belongs to the same type. We postulate that LYM2-type proteins likely function in the perception of chitin-related molecules, whereas possible functions of LYM1-type proteins remain to be elucidated.
KW - CEBiP
KW - Chitooligosaccharide
KW - GPI
KW - LYM
KW - LysM
KW - Medicago truncatula
UR - http://www.scopus.com/inward/record.url?scp=79956335210&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79956335210&partnerID=8YFLogxK
U2 - 10.1016/j.plaphy.2011.04.004
DO - 10.1016/j.plaphy.2011.04.004
M3 - Article
C2 - 21527207
AN - SCOPUS:79956335210
VL - 49
SP - 709
EP - 720
JO - Plant Physiology and Biochemistry
JF - Plant Physiology and Biochemistry
SN - 0981-9428
IS - 7
ER -