Skip to main content
main-content

01.03.2018 | Original Article | Ausgabe 2/2018

Anatomical Science International 2/2018

Unfolding of the myosin head by purealin in glycerol

Zeitschrift:
Anatomical Science International > Ausgabe 2/2018
Autoren:
Jiro Takito, Jun’ichi Kobayashi, Masanori Nakamura, Yasushi Ohizumi, Yoshiaki Nonomura

Abstract

Purealin is a small bioactive compound obtained from the marine sponge. The compound modulates various types of ATPase activity of myosin from skeletal muscle, cardiac muscle, and smooth muscle. To elucidate the structural basis of these effects of purealin on myosin ATPases, we examined the effect of purealin on the conformation of skeletal muscle myosin in aqueous solution and in glycerol. Analysis of the circular dichroism spectrum of subfragment 1, a single-headed fragment of myosin, revealed that in 10% glycerol purealin decreased the β-sheet content of S1, but in aqueous solution it had little effect on the secondary structure of S1. A myosin monomer conforms to two pear-like globular heads attached to a long tail. Electron microscopy observations with rotary shadowing revealed that purealin unfolded each globular head to an extended single strand. The tips of the unfolded strand bound each other and formed a ring in one molecule. These results suggest that binding of purealin affects the critical parameters of myosin folding.

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

★ PREMIUM-INHALT
e.Med Interdisziplinär

Mit e.Med Interdisziplinär erhalten Sie Zugang zu allen CME-Fortbildungen und Fachzeitschriften auf SpringerMedizin.de. Zusätzlich können Sie eine Zeitschrift Ihrer Wahl in gedruckter Form beziehen – ohne Aufpreis.

Literatur
Über diesen Artikel

Weitere Artikel der Ausgabe 2/2018

Anatomical Science International 2/2018 Zur Ausgabe