Recombinant Flax Lectin from Legume Family: Structure Modeling and Analysis of Posttranslational Modifications.

Area of Science:

• Plant Molecular Biology
• Biochemistry

Background:

• Legume lectins are known carbohydrate-binding proteins.
• Their role in normal plant cell physiology remains largely unknown.
• Previous transcriptomic analysis revealed differential lectin gene expression in flax.

Purpose of the Study:

• To investigate the function of Legume lectins in flax primary cell walls.
• To characterize the recombinant flax lectin Lus10021117.
• To identify post-translational modifications of Lus10021117.

Main Methods:

• Transcriptomic data analysis of flax stem tissues.
• Recombinant protein production in Nicotiana benthamiana.
• Identification of protein glycoforms, dimerization, and phosphorylation.

Main Results:

• Three Legume lectin genes showed increased expression in primary cell wall tissues.
• Recombinant Lus10021117 was successfully produced.
• Multiple glycoforms were identified, with one forming non-covalent dimers.
• Phosphorylation of Lus10021117 was demonstrated for the first time.

Conclusions:

• Legume lectins, including Lus10021117, are potentially involved in flax primary cell wall physiology.
• The characterization of Lus10021117 provides a foundation for further functional studies.
• Post-translational modifications like glycosylation, dimerization, and phosphorylation may influence lectin function in plants.