Abstract
Small signaling peptides (SSPs) are a class of short peptides playing critical roles in plant growth and development. SSPs are also involved in the phytohormone signaling pathway. However, identification of mature SSPs is still a technical challenge because of their extremely low concentrations in plant tissue and complicated interference by many other metabolites. Here, we report an optimized protocol to extract SSPs based on protoplast extraction and to analyze SSPs based on tandem mass spectrometry peptidomics. Using plant protoplasts as the material, soluble peptides were directly extracted into phosphate buffer. The interference of non-signaling peptides was significantly decreased. Moreover, we applied the protocol to identify potential SSPs in auxin treated wild type and auxin biosynthesis defective mutant yuc2yuc6. Over 100 potential SSPs showed a response to auxin in Arabidopsis thaliana.
Highlights
Small signaling peptides (SSPs) are a class of short peptides acting as signal molecules mediating cell-to-cell communication, regulation in plant growth and development, and plant response to the changing environment [1]
Frozen plant tissues were thoroughly ground into powder and the tissue powder was added into different lysate buffers with the same volume to extract total-protein
Our study indicated that extracting protein and peptides from plant protoplast is feasible
Summary
Small signaling peptides (SSPs) are a class of short peptides acting as signal molecules mediating cell-to-cell communication, regulation in plant growth and development, and plant response to the changing environment [1]. Similar to the conventional phytohormones, SSPs have physiological functions through perception by their specific receptors via certain signal transduction pathways. It is gradually accepted that SSPs are a new class of phytohormones [2]. SSPs generally appear as mature peptides with less than 20 amino acid residues, produced by selective action of peptidases on a larger precursor or by degrading from the proteolytic enzymes [3]. SSPs can function locally through intracellular signaling or be delivered to the extracellular spaces. SSPs can be structurally categorized into two groups: secreted peptides and non-secreted peptides
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