A "neural" enzyme in nonbilaterian animals and algae: preneural origins for peptidylglycine α-amidating monooxygenase

Attenborough, Rosalind M.F., Hayward, David C., V. Kitahara, Marcelo, Miller, David J., and Ball, Eldon E. (2012) A "neural" enzyme in nonbilaterian animals and algae: preneural origins for peptidylglycine α-amidating monooxygenase. Molecular Biology and Evolution, 29 (10). pp. 3095-3109.

[img] PDF (Published Version) - Published Version
Restricted to Repository staff only

View at Publisher Website: http://dx.doi.org/10.1093/molbev/mss114
 
23
4


Abstract

Secreted peptides, produced by enzymatic processing of larger precursor molecules, are found throughout the animal kingdom and play important regulatory roles as neurotransmitters and hormones. Many require a carboxy-terminal modification, involving the conversion of a glycine residue into an alpha-amide, for their biological activity. Two sequential enzymatic activities catalyze this conversion: a monooxygenase (peptidylglycine α-hydroxylating monooxygenase or PHM) and an amidating lyase (peptidyl-α-hydroxyglycine α-amidating lyase or PAL). In vertebrates, these activities reside in a single polypeptide known as peptidylglycine α-amidating monooxygenase (PAM), which has been extensively studied in the context of neuropeptide modification. Bifunctional PAMs have been reported from some invertebrates, but the phylogenetic distribution of PAMs and their evolutionary relationship to PALs and PHMs is unclear. Here, we report sequence and expression data for two PAMs from the coral Acropora millepora (Anthozoa, Cnidaria), as well as providing a comprehensive survey of the available sequence data from other organisms. These analyses indicate that bifunctional PAMs predate the origins of the nervous and endocrine systems, consistent with the idea that within the Metazoa their ancestral function may have been to amidate epitheliopeptides. More surprisingly, the phylogenomic survey also revealed the presence of PAMs in green algae (but not in higher plants or fungi), implying that the bifunctional enzyme either predates the plant/animal divergence and has subsequently been lost in a number of lineages or perhaps that convergent evolution or lateral gene transfer has occurred. This finding is consistent with recent discoveries that other molecules once thought of as "neural" predate nervous systems.

Item ID: 24175
Item Type: Article (Research - C1)
ISSN: 1537-1719
Keywords: peptidylglycine alpha-amidating monooxygenase, PAM, peptide amidation, Acropora millepora, phylogenomics
Funders: Australian Research Council (ARC)
Date Deposited: 05 Dec 2012 05:32
FoR Codes: 06 BIOLOGICAL SCIENCES > 0608 Zoology > 060802 Animal Cell and Molecular Biology @ 25%
06 BIOLOGICAL SCIENCES > 0604 Genetics > 060409 Molecular Evolution @ 50%
06 BIOLOGICAL SCIENCES > 0603 Evolutionary Biology > 060399 Evolutionary Biology not elsewhere classified @ 25%
SEO Codes: 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
Downloads: Total: 4
More Statistics

Actions (Repository Staff Only)

Item Control Page Item Control Page