RRC ID 15322
Author Van Hove J, Fouquaert E, Smith DF, Proost P, Van Damme EJ.
Title Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana.
Journal Biochem Biophys Res Commun
Abstract The Euonymus lectin (EUL) domain was recognized as the structural motif for a novel class of putative carbohydrate binding proteins. Confocal microscopy demonstrated that the lectin from Euonymus europaeus (EEA) as well as the EUL protein from Arabidopsis thaliana (ArathEULS3) are located in the nucleocytoplasmic compartment of the plant cell. ArathEULS3 as well as its EUL domain were successfully expressed in Pichia pastoris and purified. The EUL domain from Arabidopsis interacts with glycan structures containing Lewis Y, Lewis X and lactosamine, indicating that it can be considered a true lectin domain. Despite the high sequence identity between the EUL domains in EEA and ArathEULS3, both domains recognize different carbohydrate structures.
Volume 414(1)
Pages 101-5
Published 2011-10-14
DOI 10.1016/j.bbrc.2011.09.031
PII S0006-291X(11)01620-2
PMID 21945438
PMC PMC3195871
MeSH Amino Acid Sequence Amino Sugars / chemistry Amino Sugars / metabolism Antimicrobial Cationic Peptides / chemistry Antimicrobial Cationic Peptides / genetics Antimicrobial Cationic Peptides / metabolism* Arabidopsis / chemistry Arabidopsis / genetics Arabidopsis / metabolism* Arabidopsis Proteins / chemistry Arabidopsis Proteins / genetics Arabidopsis Proteins / metabolism* Cell Nucleus / metabolism Cloning, Molecular Cytoplasm / metabolism Lectins / chemistry Lectins / genetics Lectins / metabolism* Lewis Blood Group Antigens / chemistry Lewis Blood Group Antigens / metabolism Lewis X Antigen / chemistry Lewis X Antigen / metabolism Molecular Sequence Data Pichia Plant Lectins / chemistry Plant Lectins / genetics Plant Lectins / metabolism* Protein Structure, Tertiary
IF 2.985
Times Cited 20
WOS Category BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Arabidopsis / Cultured plant cells, genes pda02666