CLE14/CLE20 peptides may interact with CLAVATA2/CORYNE receptor-like kinases to irreversibly inhibit cell division in the root meristem of Arabidopsis |
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Authors: | Ling Meng Lewis J Feldman |
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Institution: | (1) Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, CA 94720-3102, USA; |
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Abstract: | Towards an understanding of the interacting nature of the CLAVATA (CLV) complex, we predicted the 3D structures of CLV3/ESR-related
(CLE) peptides and the ectodomain of their potential receptor proteins/kinases, and docking models of these molecules. The
results show that the ectodomain of CLV1 can form homodimers and that the 12-/13-amino-acid CLV3 peptide fits into the binding
clefts of the CLV1 dimers. Our results also demonstrate that the receptor domain of CORYNE (CRN), a recently identified receptor-like
kinase, binds tightly to the ectodomain of CLV2, and this likely leads to an increased possibility for docking with CLV1.
Furthermore, our docking models reveal that two CRN-CLV2 ectodomain heterodimers are able to form a tetramer receptor complex.
Peptides of CLV3, CLE14, CLE19, and CLE20 are also able to bind a potential CLV2-CRN heterodimer or heterotetramer complex.
Using a cell-division reporter line, we found that synthetic 12-amino-acid CLE14 and CLE20 peptides inhibit, irreversibly,
root growth by reducing cell division rates in the root apical meristem, resulting in a short-root phenotype. Intriguingly,
we observed that exogenous application of cytokinin can partially rescue the short-root phenotype induced by over-expression
of either CLE14 or CLE20 in planta. However, cytokinin treatment does not rescue the short-root phenotype caused by exogenous application of the synthetic
CLE14/CLE20 peptides, suggesting a requirement for a condition provided only in living plants. These results therefore imply
that the CLE14/CLE20 peptides may act through the CLV2-CRN receptor kinase, and that their availabilities and/or abundances
may be affected by cytokinin activity in planta. |
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