Effect of organic cryosolvents on actin structures and actin/[MATH]-actinin binding geometries

Autor: E. Pajot-Augy, M. A. V. Axelos
Jazyk: angličtina
Rok vydání: 1993
Předmět:
Zdroj: Journal de Physique IV Proceedings
Journal de Physique IV Proceedings, EDP Sciences, 1993, 03 (C8), pp.C8-241-C8-244. ⟨10.1051/jp4:1993846⟩
ISSN: 1155-4339
1764-7177
DOI: 10.1051/jp4:1993846⟩
Popis: Cryopreservation procedures of living cells involve the use of organic solvents against freezing damage. An efficient cryoprotection might be achieved by obtaining a cytoplasmic gel able to reduce water flux and avoid crystallization. Small angle X-ray scattering experiments were performed at LURE (Orsay, France) to investigate the effects of 1,2- propanediol and glycerol on the structure of actin, a major cytoplasmic protein, and on the binding geometries of actin to [MATH]-actinin, an interconnecting protein. In the presence of 1,2-propanediol, monomeric G-actin exhibits oligomerization into short rod-like structures very close to that of salt-polymerized actin filaments (F-actin). In the presence of [MATH]-actinin. F-actin filaments aggregate into thick and tight bundles. The scattering pattern in the presence of propanediol suggests a "ladder-like" structure with a tilt angle of the [MATH]-actinin molecule relative to F-actin filaments. This angle is even larger with glycerol. The resulting loose structures favor the formation of a microporous network. All these results support previous electron microscopy observations and the structural mechanisms deduced from rheological measurements.
Databáze: OpenAIRE