Calmodulin EF-hand peptides as Ca 2+ -switchable recognition tags

Calmodulin is a representative calcium-binding protein comprised of four Ca -binding motifs with a helix-loop-helix structure (EF-hands). In this study, we clarified the potential of peptide segments derived from the third and fourth EF-hands (EF3 and EF4) to act as recognition tags. Through an anal...

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Veröffentlicht in:Biopolymers 2017-01, Vol.108 (1)
Hauptverfasser: Oku, Akihiko, Imanishi, Miki, Noshiro, Daisuke, Murayama, Tomo, Takeuchi, Toshihide, Nakase, Ikuhiko, Futaki, Shiroh
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Sprache:eng
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Zusammenfassung:Calmodulin is a representative calcium-binding protein comprised of four Ca -binding motifs with a helix-loop-helix structure (EF-hands). In this study, we clarified the potential of peptide segments derived from the third and fourth EF-hands (EF3 and EF4) to act as recognition tags. Through an analysis of the mode of disulfide formation among cysteines inserted at the N- or C-terminus of these peptide segments, EF3 and EF4 peptides were suggested to form a heterodimer with a topology similar to that in the wild-type protein. Heterodimer formation was shown to be a function of the Ca concentration, suggesting that these structures may be used as Ca -switchable recognition tags. An example of an "EF-tag" system involving the membrane fusion of liposomes decorated with EF3 and EF4 peptides is presented. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2016.
ISSN:1097-0282
DOI:10.1002/bip.22937