The Tobacco Lectin, Prototype of the Family of Nictaba-Related Proteins

Author(s): Annelies Delporte , Sofie Van Holle , Nausicaa Lannoo , Els J.M. Van Damme .

Journal Name: Current Protein & Peptide Science

Volume 16 , Issue 1 , 2015

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Abstract:

In the last decade, a new class of low abundant plant l ectins was identified. These proteins are expressed after exposure of the plant to different stress factors and changing environmental conditions, and therefore are referred to as “inducible” lectins. Interestingly, these lectins accumulate in the nucleocytoplasmic compartment of plant cells. At present at least six carbohydrate recognition domains have been identified within the group of nucleocytoplasmic plant lectins. This review will focus on a group of proteins that show homology to the Nicotiana tabacum (tobacco) agglutinin or Nictaba. The tobacco lectin is a 38 kDa nucleocytoplasmic protein which is only expressed upon treatment with jasmonate-related compounds or after insect herbivory. The lectin exhibits specificity towards GlcNAc, but also reacts with N-glycan structures. Extensive searches revealed that Nictaba-related sequences are widespread in the plant kingdom. Analyses of the different transcriptome databases showed that the Nictaba domain is often part of chimeric proteins comprising one or more Nictaba domain( s) fused to unrelated N- and C-terminal domains with (un)known function. At present only few proteins of these Nictaba-related proteins have been studied and characterized for their biological properties and physiological role. Despite the sequence similarity and the conserved amino acids constituting the binding site, the Nictaba domain has a promiscuous carbohydrate binding site capable of interacting with different carbohydrate motifs, suggesting that subtle changes in the vicinity of the binding site can alter its sugar specificity.

Keywords: Carbohydrate, insect herbivory, jasmonate signaling, N-glycan, Nictaba, plant lectin.

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Article Details

VOLUME: 16
ISSUE: 1
Year: 2015
Page: [5 - 16]
Pages: 12
DOI: 10.2174/1389203716666150213154107

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