Solution NMR studies of the plant peptide hormone CEP inform function

被引：45

作者：

Bobay, Benjamin G. ^{[1
]}

DiGennaro, Peter ^{[2
]}

Scholl, Elizabeth ^{[2
]}

Imin, Nijat ^{[3
]}

Djordjevic, Michael A. ^{[3
]}

Bird, David Mck ^{[2
,4
]}

机构：

[1] NC State Univ, Dept Mol & Struct Biochem, Raleigh, NC 27695 USA

[2] NC State Univ, Dept Plant Pathol, Raleigh, NC 27695 USA

[3] Australian Natl Univ, Plant Sci Div, Res Sch Biol, Coll Med Biol & Environm, Canberra, ACT 0200, Australia

[4] NC State Univ, Bioinformat Res Ctr, Raleigh, NC 27695 USA

来源：

FEBS LETTERS | 2013年 / 587卷 / 24期

基金：

澳大利亚研究理事会; 美国国家科学基金会;

关键词：

NMR; Molecular dynamic; CEP; Root-knot nematode; Peptide; CLE; Meloidogyne; AUTOMATED NOE ASSIGNMENT; SECRETED PEPTIDE; SIGNAL PEPTIDES; IDENTIFICATION; PREDICTION;

D O I：

10.1016/j.febslet.2013.10.033

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3979 / 3985

页数：7

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