{"refrec":{"BRefID":310427,"RR":"<b>Madio, B.; Peigneur, S.; Chin, Y.K.Y.; Hamilton, B.; Henriques, S.T.; Smith, J.J.; Cristofori-Armstrong, B.; Dekan, Z.; Boughton, B.A.; Alewood, P.F.; Tytgat, J.; King, G.F.; Undheim, E.A.B.</b> (2018). PHAB toxins: a unique family of predatory sea anemone toxins evolving via intra-gene concerted evolution defines a new peptide fold. <i>Cellular and molecular life sciences 75(24)</i>: 4511-4524. <a href=\"https://dx.doi.org/10.1007/s00018-018-2897-6\" target=\"_blank\">https://dx.doi.org/10.1007/s00018-018-2897-6</a>","BEntID":302758,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Cellular and molecular life sciences 75(24)</i>: 4511-4524. <a href=\"https://dx.doi.org/10.1007/s00018-018-2897-6\" target=\"_blank\">https://dx.doi.org/10.1007/s00018-018-2897-6</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Madio, B.; Peigneur, S.; Chin, Y.K.Y.; Hamilton, B.; Henriques, S.T.; Smith, J.J.; Cristofori-Armstrong, B.; Dekan, Z.; Boughton, B.A.; Alewood, P.F.; Tytgat, J.; King, G.F.; Undheim, E.A.B.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Madio, B. <i>et al.</i>","Englishabstract":"Sea anemone venoms have long been recognized as a rich source of peptides with interesting pharmacological and structural properties, but they still contain many uncharacterized bioactive compounds. Here we report the discovery, three-dimensional structure, activity, tissue localization, and putative function of a novel sea anemone peptide toxin that constitutes a new, sixth type of voltage-gated potassium channel (KV) toxin from sea anemones. Comprised of just 17 residues, κ-actitoxin-Ate1a (Ate1a) is the shortest sea anemone toxin reported to date, and it adopts a novel three-dimensional structure that we have named the Proline-Hinged Asymmetric β-hairpin (PHAB) fold. Mass spectrometry imaging and bioassays suggest that Ate1a serves a primarily predatory function by immobilising prey, and we show this is achieved through inhibition of Shaker-type KV channels. Ate1a is encoded as a multi-domain precursor protein that yields multiple identical mature peptides, which likely evolved by multiple domain duplication events in an actinioidean ancestor. Despite this ancient evolutionary history, the PHAB-encoding gene family exhibits remarkable sequence conservation in the mature peptide domains. We demonstrate that this conservation is likely due to intra-gene concerted evolution, which has to our knowledge not previously been reported for toxin genes. We propose that the concerted evolution of toxin domains provides a hitherto unrecognised way to circumvent the effects of the costly evolutionary arms race considered to drive toxin gene evolution by ensuring efficient secretion of ecologically important predatory toxins.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"PHAB toxins: a unique family of predatory sea anemone toxins evolving via intra-gene concerted evolution defines a new peptide fold","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Neurotoxin; Ion channel; Mass spectrometry imaging; 3D structure;Concerted evolution; Extreme resolution mass spectrometry imaging;On-tissue reduction alkylation","OtherDescriptors":null,"Notes":null,"AnaPub":2018,"MonPub":null,"DateUpdate":"2019-04-24","DateCreate":"2019-04-17","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000448955600003","VABBcode":null,"OpenAcc":0,"DOI":"10.1007/s00018-018-2897-6"},"refs":null,"anarec":{"AnaID":310427,"PubliDate":2018,"Pagination":"4511-4524","XtraPublOfAnaID":null,"ISBN":null,"Volume":"75","Issue":"24","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":235306,"SerRR":"Cellular and molecular life sciences. 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