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Sialic acid-binding dwarf elder four-chain lectin displays nucleic acid N-glycosidase activity.
Iglesias, Rosario; Citores, Lucía; Ferreras, J Miguel; Pérez, Yolanda; Jiménez, Pilar; Gayoso, Manuel J; Olsnes, Sjur; Tamburino, Rachele; Di Maro, Antimo; Parente, Augusto; Girbés, Tomás.
Afiliação
  • Iglesias R; Departamento de Bioquímica y Biología Molecular, Universidad de Valladolid, Spain.
Biochimie ; 92(1): 71-80, 2010 Jan.
Article em En | MEDLINE | ID: mdl-19799962
Sialic acid-binding dwarf elder agglutinin (SEA) present only in rhizomes of the medicinal plant Sambucus ebulus L., was found to be a tetrameric glycoprotein consisting of two covalently-associated dimers of an enzymic A chain with rRNA N-glycosidase activity (EC 3.2.2.22) linked to a B chain with agglutinin properties. The lectin inhibited protein synthesis by a cell-free system and depurinated ribosomes. Cloning of the corresponding gene and molecular modeling of the deduced amino acid sequence demonstrated that SEA has a three-dimensional structure which resembles that reported for other two tetrameric type 2 RIPs from Sambucus (SNAI and SSA). The lectin agglutinated red blood cells and displayed sugar affinity for sialic acid residues apart from d-galactose, binding to the mucin-producing gut goblet cells. Since sialic acid is present in animal cells, especially in epithelial lining gut cells, but not in plants, SEA could play a role in the defense against insect attack. The nucleotide sequence reported in this paper has been submitted to the GenBank nucleotide database under accession number AM981401.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ácidos Nucleicos / Ácido N-Acetilneuramínico / Sambucus / Lectinas de Plantas / Glicosídeo Hidrolases Limite: Animals Idioma: En Revista: Biochimie Ano de publicação: 2010 Tipo de documento: Article País de afiliação: Espanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ácidos Nucleicos / Ácido N-Acetilneuramínico / Sambucus / Lectinas de Plantas / Glicosídeo Hidrolases Limite: Animals Idioma: En Revista: Biochimie Ano de publicação: 2010 Tipo de documento: Article País de afiliação: Espanha