Solution NMR studies of the plant peptide hormone CEP inform function

Benjamin G. Bobay; Peter Digennaro; Elizabeth Scholl; Nijat Imin; Michael A. Djordjevic; David McK Bird

doi:10.1016/j.febslet.2013.10.033

Solution NMR studies of the plant peptide hormone CEP inform function

Benjamin G. Bobay, Peter Digennaro, Elizabeth Scholl, Nijat Imin, Michael A. Djordjevic, David McK Bird

Western Sydney University

Research output: Contribution to journal › Article › peer-review

45 Citations (Scopus)

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.

Original language	English
Pages (from-to)	3979-3985
Number of pages	7
Journal	FEBS Letters
Volume	587
Issue number	24
DOIs	https://doi.org/10.1016/j.febslet.2013.10.033
Publication status	Published - 2013

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10.1016/j.febslet.2013.10.033

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title = "Solution NMR studies of the plant peptide hormone CEP inform function",

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.",

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AU - Bobay, Benjamin G.

AU - Digennaro, Peter

AU - Scholl, Elizabeth

AU - Imin, Nijat

AU - Djordjevic, Michael A.

AU - McK Bird, David

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

UR - https://hdl.handle.net/1959.7/uws:76490

U2 - 10.1016/j.febslet.2013.10.033

DO - 10.1016/j.febslet.2013.10.033

M3 - Article

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VL - 587

SP - 3979

EP - 3985

JO - FEBS Letters

JF - FEBS Letters

IS - 24

ER -

Solution NMR studies of the plant peptide hormone CEP inform function

Abstract

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