Identification of a neuropeptide precursor protein that gives rise to a "cocktail" of peptides that bind Cu(II) and generate metal-linked dimers

Jones, Christopher E., Zandawala, Meet, Semmens, Dean C., Anderson, Sarah, Hanson, Graeme R., Janies, Daniel A. and Elphick, Maurice R. (2016) Identification of a neuropeptide precursor protein that gives rise to a "cocktail" of peptides that bind Cu(II) and generate metal-linked dimers. Biochimica et Biophysica Acta (BBA) - General Subjects, 1860 1: 57-66. doi:10.1016/j.bbagen.2015.10.008


Author Jones, Christopher E.
Zandawala, Meet
Semmens, Dean C.
Anderson, Sarah
Hanson, Graeme R.
Janies, Daniel A.
Elphick, Maurice R.
Title Identification of a neuropeptide precursor protein that gives rise to a "cocktail" of peptides that bind Cu(II) and generate metal-linked dimers
Journal name Biochimica et Biophysica Acta (BBA) - General Subjects   Check publisher's open access policy
ISSN 0304-4165
1872-8006
Publication date 2016-01-01
Year available 2016
Sub-type Article (original research)
DOI 10.1016/j.bbagen.2015.10.008
Open Access Status Not Open Access
Volume 1860
Issue 1
Start page 57
End page 66
Total pages 10
Place of publication Amsterdam, The Netherlands
Publisher Elsevier
Language eng
Formatted abstract
Background
Neuropeptides with an Amino Terminal Cu(II), Ni(II) Binding (ATCUN) motif (H2N-xxH) bind Cu(II)/Ni(II) ions. Here we report the novel discovery of a neuropeptide precursor that gives rise to a “cocktail” of peptides that bind Cu(II)/Ni(II) and form ternary complexes — the L-type SALMFamide precursor in the starfish Asterias rubens.

Methods
Echinoderm transcriptome sequence data were analysed to identify transcripts encoding precursors of SALMFamide-type neuropeptides. The sequence of the L-type SALMFamide precursor in the starfish Asterias rubens was confirmed by cDNA sequencing and peptides derived from this precursor (e.g. AYHSALPF-NH2, GYHSGLPF-NH2 and LHSALPF-NH2) were synthesized. The ability of these peptides to bind metals was investigated using UV/Vis, NMR, circular dichroism and EPR spectroscopy.

Results
AYHSALPF-NH2 and GYHSGLPF-NH2 bind Cu(II) and Ni(II) and generate metal-linked dimers to form ternary complexes with LHSALPF-NH2. Investigation of the evolutionary history of the histidine residue that confers these properties revealed that it can be traced to the common ancestor of echinoderms, which is estimated to have lived ~ 500 million years ago. However, L-type precursors comprising multiple SALMFamides with the histidine residue forming an ATCUN motif appears to be a feature that has evolved uniquely in starfish (Asteroidea).

General Significance
The discovery of a SALMFamide-type neuropeptide precursor protein that gives rise to a “cocktail” of peptides that bind metal ions and generate metal-linked dimers provides a new insight on ATCUN motif-containing neuropeptides. This property of L-type SALMFamides in the Asteroidea may be associated with a role in regulation of the unusual extra-oral feeding behaviour of starfish.
Keyword ATCUN
Copper
Echinoderm
Neuropeptide
SALMFamide
Starfish
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
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