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FEBS Lett. 2013 Dec 11;587(24):3979-85. doi: 10.1016/j.febslet.2013.10.033. Epub 2013 Nov 5.

Solution NMR studies of the plant peptide hormone CEP inform function.

Author information

1
Department of Molecular and Structural Biochemistry, NC State University, Raleigh, NC 27695, United States.

Abstract

The C-terminally Encoded Peptide (CEP) family of regulatory peptides controls root development in vascular plants. Here, we present the first NMR structures of CEP. We show that root-knot nematode (RKN: Meloidogyne spp.) also encodes CEP, presumably to mimic plant CEP as part of their stereotypic, parasitic interaction with vascular plants. Molecular dynamics simulations of plant- and nematode-encoded CEP displaying known posttranslational modifications (PTM) provided insight into the structural effects of PTM and the conformational plasticity and rigidity of CEP. Potential mechanisms of action are discussed with respect to the structure and sampling of conformational space.

KEYWORDS:

CEP; CLE; Meloidogyne; Molecular dynamic; NMR; Peptide; Root-knot nematode

PMID:
24211833
DOI:
10.1016/j.febslet.2013.10.033
[Indexed for MEDLINE]
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