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On the localization of FKBP25 in T‐lymphocytes
Author(s) -
Rivière Sylvie,
Ménez André,
Galat Andrzej
Publication year - 1993
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(93)81173-w
Subject(s) - jurkat cells , polyclonal antibodies , dna , microbiology and biotechnology , biology , blot , peptide sequence , biochemistry , antibody , chemistry , t cell , genetics , immune system , gene
Using polyclonal rabbit antibodies against bovine FKBP25, NEPHGE/SDS‐PAGE and Western blotting we demonstrate that the rapamycin‐specific immunophilin FKBP25 is present in T‐lymphoma Jurkat cells. Subsequent fractionations of the soluble Jurkat cell proteins have revealed that FKBP25 predominantly occurs in the nuclear fraction. FKBP25 has the ability to bind to DNA. The FKBP25/DNA complex can be dissociated in the presence of a high salt concentration. FKBP12, which shares high amino acid sequence homology to the C‐tenninal domain of FKBP25, has no tendency to bind to DNA. CD‐constrained predictions of the secondary structures in FKBP25 suggest that an amphipathic helix‐loop‐helix occurs in the N‐terminal part of the protein and may account for its binding to DNA.