Dual assay for MCLV3 activity reveals structure-activity relationship of CLE peptides.

Biochem Biophys Res Commun

Graduate School of Bioagricultural Science, Nagoya University, Chikusa, Nagoya, Japan.

Published: December 2008

AI Article Synopsis

  • MCLV3 is a functional peptide from the CLV3 precursor protein that interacts with the CLV1/CLV2 receptor complex to regulate stem cell activity in plant growth.
  • The study examined how changes in MCLV3's structure, specifically through alanine substitutions, affected root growth in Arabidopsis, revealing similarities to another peptide, TDIF.
  • Additionally, competitive receptor binding assays demonstrated that specific terminal residues of MCLV3 are crucial for its activity and binding to the CLV1 receptor, highlighting important aspects of its structure-activity relationship.

Article Abstract

The dodecapeptide MCLV3 is a functional peptide, derived from the CLV3 precursor protein, which is a candidate ligand of the CLV1/CLV2 receptor complex that restricts the stem cell population in the shoot apical meristem (SAM). MCLV3 can induce shoot and root meristem consumption, the typical phenotype of transgenic plants overexpressing CLV3. We investigated the bioactivities of a series of alanine-substituted MCLV3 and related peptides on the root growth of Arabidopsis. The structure-activity relationship (SAR) of MCLV3 had high similarity with that of tracheary element differentiation inhibitory factor (TDIF). We also evaluated the binding activities of the peptides by a competitive receptor binding assay using tritiated MCLV3 and the membrane fraction of a tobacco BY-2 cell line overexpressing the MCLV3 ectodomain. This dual assay, combining a biological and receptor binding assay for evaluating the activities of MCLV3-related peptides, uncovered the SAR of MCLV3, and indicated that the terminal residues play critical roles in exerting its activity and are important for specific binding to the receptor, CLV1.

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http://dx.doi.org/10.1016/j.bbrc.2008.09.139DOI Listing

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