HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Froy, O. Articles by Gurevitz, M. Search for Related Content PubMed PubMed Citation Articles by Froy, O. Articles by Gurevitz, M.

Membrane potential modulators: a thread of scarlet from plants to humans

^a Department of Plant Sciences, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat-Aviv 69978, Tel Aviv, Israel

The preservation along evolution of specific core motifs in proteins of diverse functions and taxonomic origins pinpoints a possible developmental advantage at the structural level. Such a preservation was observed in a group of membrane potential modulators including plant -thionins, scorpion toxins, insect and scorpion defensins, bee venom apamin and MCD peptide, snake sarafotoxins, and human endothelins. These substances are short polypeptides of various lengths and nonhomologous sequences that affect organisms of distant phyla. Despite the structural differences, comparative analysis reveals commonality at three levels: 1) effect on membrane potential; 2) a common cysteine-stabilized -helical (CSH) motif; and 3) similar gene organization (except for insect defensins), i.e., an intron that splits a codon toward the end of the leader sequence. We thus propose that these modulators, divided into two groups differing in their CSH motif orientation, have either diverged from two independent ancestors or have evolved by gene diversification via exon shuffling and subsequent modifications. To enforce protein synthesis through the secretory pathway and enable disulfide bond formation and secretion, insertion sites downstream of preexisting leader sequences have been a prerequisite. What seems advantageous for evolution, may also be exploited in attempts to `accelerate evolution' by protein design using the conserved CSH core as a suitable scaffold for reshaping molecular exteriors.—Froy, O., Gurevitz, M. Membrane potential modulators: a thread of scarlet from plants to humans. FASEB J. 12, 1793–1796 (1998)

Key Words: neurotoxins • structural motifs • evolution • MCD peptide

This article has been cited by other articles:

				L. Cohen, N. Lipstein, I. Karbat, N. Ilan, N. Gilles, R. Kahn, D. Gordon, and M. Gurevitz Miniaturization of Scorpion {beta}-Toxins Uncovers a Putative Ancestral Surface of Interaction with Voltage-gated Sodium Channels J. Biol. Chem., May 30, 2008; 283(22): 15169 - 15176. [Abstract] [Full Text] [PDF]

				P. Mergaert, K. Nikovics, Z. Kelemen, N. Maunoury, D. Vaubert, A. Kondorosi, and E. Kondorosi A Novel Family in Medicago truncatula Consisting of More Than 300 Nodule-Specific Genes Coding for Small, Secreted Polypeptides with Conserved Cysteine Motifs Plant Physiology, May 1, 2003; 132(1): 161 - 173. [Abstract] [Full Text] [PDF]

				M. GUREVITZ, D. GORDON, S. BEN-NATAN, M. TURKOV, and O. FROY Diversification of neurotoxins by C-tail wiggling': a scorpion recipe for survival FASEB J, May 1, 2001; 15(7): 1201 - 1205. [Abstract] [Full Text] [PDF]