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 (Kapp) 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. © 1992.
Kooijman, M., Bloemendal, M., Traub, P., & van Grondelle, R. (1992). Fluorescence study of the nucleic acid binding site of vimentin. FEBS Letters, 302(2), 177–180. https://doi.org/10.1016/0014-5793(92)80434-I