Interactions of elongation factor 2 with the cytoskeleton and interference with DNase I binding to actin

Bektas M., Nurten R., Sayers Z., Bermek E.

EUROPEAN JOURNAL OF BIOCHEMISTRY, cilt.256, sa.1, ss.142-147, 1998 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 256 Sayı: 1
  • Basım Tarihi: 1998
  • Doi Numarası: 10.1046/j.1432-1327.1998.2560142.x
  • Dergi Adı: EUROPEAN JOURNAL OF BIOCHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.142-147
  • İstanbul Üniversitesi Adresli: Evet

Özet

Interactions of elongation factor 2 (EF-2) with G-actin and F-actin in vitro were investigated using viscosimetry, gel filtration and electron microscopy. Under depolymerization conditions, at a molar ratio of 0.5:1 (EF-2/F-actin subunit), F-actin is stabilised by EF-2 and filaments depolymerize about three times slower than control solutions containing only F-actin. Filament stability is improved also when EF-2 is included in the solution in the presence of DNase I. Electron micrographs and viscosity measurements indicate that EF-2 may support small bundles with a width of 2 or 3 filaments. It was established that EF-2 interacts with G-actin in vitro, and reduces G-actin inhibition of DNase I activity when it is present at a ratio of 1:1. Results are discussed in the context of possible functional significance of the interactions.