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Fluorescence study of the nucleic acid binding site of vimentin
Author(s) -
Kooijman Martin,
Bloemendal Michael,
Traub Peter,
van Grondelle Rienk
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80434-i
Subject(s) - vimentin , nucleic acid , chemistry , quenching (fluorescence) , fluorescence , tyrosine , intermediate filament , protein filament , binding site , binding constant , nucleotide , biophysics , biochemistry , biology , cytoskeleton , cell , physics , gene , immunology , immunohistochemistry , quantum mechanics
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 × 10 7 M −1 ·cm −1 vs. 2.5 ± 0.5 × 10 7 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.