Электронный каталог

Статья

Ryzhykau, Y.L.
Small-Angle X-Ray Scattering Structural Insights into Alternative Pathway of Actin Oligomerization Associated with Inactivated State / Y.L.Ryzhykau, A.I.Kuklin, [et al.] // Biochemical and Biophysical Research Communications [Electronic resource]. – 2024. – Vol. 693. – P. 149340. – URL: https://doi.org/10.1016/j.bbrc.2023.149340. – Bibliogr.: 33.

In addition to the well-known monomeric globular (G-actin) and polymeric fibrillar (F-actin) forms, actin can exist in the so-called inactivated form (I-actin). Hsp70 chaperon, prefoldin, and CCT chaperonin are required to obtain native globular state. In contrast, I-actin is spontaneously formed in the absence of intracellular folding machinery. I-actin can be obtained from G-actin by elimination of divalent ion, incubation in presence of small concentrations of denaturants, and by heat exposure. Since G-actin is a quasi-stationary, thermodynamically unstable form, it can gradually transform into inactivated state in the absence of chelating/denaturating agents or heat exposure, but the transition is much slower. I-actin was shown to associate into oligomers up to the molecular weight of 14–16 G-actin monomers, though the structure of these oligomers remains uncharacterized. This study employs small-angle X-ray scattering to reveal novel insights into the oligomerization process of such spontaneously formed inactivated actin. These oligomers are differentiated from F-actin through comparative analysis, highlighting a unique oligomerization pathway.



Спец.(статьи,препринты) = С 332.8 - Синхротронное излучение. Лазеры на свободных электронах. Получение и использование рентгеновских лучей
ОИЯИ = ОИЯИ (JINR)2024
Ключевых слов = 20/024