Fluorescence study of the nucleic acid binding site of vimentin

FEBS Letters

Kooijman, Martin³  Traub, Peter¹  van Grondelle, Rienk³  Bloemendal, Michael² 

[1] Max Planck Institute for Cell Biology, D6802 Ladenburg/Heidelberg, Germany;Free University of Amsterdam, Department of General and Analytical Chemistry, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands;Free University of Amsterdam, Department of Biophysics, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands

关键词: Intermediate filament protein;    Vimentin;    Protein fluorescence;    Nucleic acid binding protein;   

DOI  :  10.1016/0014-5793(92)80434-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A selective tyrosine fluorescence quenching is found on interaction of vimentin with poly(dT) and poly(rA). However, addition of poly(dA) does not result in tyrosine quenching. The number of nucleotides covered by vimentin upon binding(n) of poly(dT) (50 ± 4) appeared to be approximately the same as for poly(rA) (44 ± 4), while the apparent binding constant (K _app) of the latter is slightly larger (5.0 ± 2.0 × 10⁷ M⁻¹·cm⁻¹ vs. 2.5 ± 0.5 × 10⁷ M⁻¹·cm⁻¹). The finding that there exists a specific strong interaction between vimentin and nucleic acids could help in the search for cellular functions of intermediate filament proteins.

【 授权许可】

Unknown