Abstract

BackgroundCloning of the Euonymus lectin led to the discovery of a novel domain that also occurs in some stress-induced plant proteins. The distribution and the diversity of proteins with an Euonymus lectin (EUL) domain were investigated using detailed analysis of sequences in publicly accessible genome and transcriptome databases.ResultsComprehensive in silico analyses indicate that the recently identified Euonymus europaeus lectin domain represents a conserved structural unit of a novel family of putative carbohydrate-binding proteins, which will further be referred to as the Euonymus lectin (EUL) family. The EUL domain is widespread among plants. Analysis of retrieved sequences revealed that some sequences consist of a single EUL domain linked to an unrelated N-terminal domain whereas others comprise two in tandem arrayed EUL domains. A new classification system for these lectins is proposed based on the overall domain architecture. Evolutionary relationships among the sequences with EUL domains are discussed.ConclusionThe identification of the EUL family provides the first evidence for the occurrence in terrestrial plants of a highly conserved plant specific domain. The widespread distribution of the EUL domain strikingly contrasts the more limited or even narrow distribution of most other lectin domains found in plants. The apparent omnipresence of the EUL domain is indicative for a universal role of this lectin domain in plants. Although there is unambiguous evidence that several EUL domains possess carbohydrate-binding activity further research is required to corroborate the carbohydrate-binding properties of different members of the EUL family.

Highlights

  • Cloning of the Euonymus lectin led to the discovery of a novel domain that occurs in some stress-induced plant proteins

  • The identification of the Euonymus lectin (EUL) family provides the first evidence for the occurrence in terrestrial plants of a highly conserved plant specific domain

  • The widespread distribution of the EUL domain strikingly contrasts the more limited or even narrow distribution of most other lectin domains found in plants

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Summary

Introduction

Cloning of the Euonymus lectin led to the discovery of a novel domain that occurs in some stress-induced plant proteins. Though applicable to the majority of all previously studied plant lectins, novel concepts had to be developed after the identification of several novel hormone or stressresponsive lectins By virtue of their subcellular location and specificity this new class of lectins is at least in principle capable of interacting with endogenous receptors in the cytoplasmic/nuclear compartment of the plant cell [2,5,6,7]. Based on a comprehensive analysis of the data generated by biochemical, molecular biological and plant physiological studies, and genome/transcriptome/proteome surveys it was proposed recently that plants express lectins that mediate specific protein-carbohydrate interactions in the cytoplasm and nucleus of the plant cell, and by doing so might play an important role in regulatory processes and/or cell signalling [8,9]. Five families of such inducible nucleocytoplasmic lectins have been identified [9]

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