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Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H‐NS, a bacterial nucleoid protein.
Author(s) -
Timchenko T.,
Bailone A.,
Devoret R.
Publication year - 1996
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1996.tb00772.x
Subject(s) - nucleoid , biology , escherichia coli , escherichia coli proteins , dna , dna binding protein , bacterial protein , enterobacteriaceae , bacteria , microbiology and biotechnology , genetics , biochemistry , gene , transcription factor
In an Escherichia coli mutant devoid of H‐NS, a bacterial nucleoid protein, mouse protein Btcd was able to substitute for H‐NS in two tested functions. It restored cell motility and repression of the expression of the bgl operon. Btcd1, a mutant Btcd protein deleted of its zinc finger and thus having reduced DNA binding, failed to substitute for H‐NS. Mouse protein Btcd was shown to repress the bgl operon at the level of transcription initiation and to bind preferentially to a curved DNA fragment encompassing the bgl promoter. These effects of Btcd on bacterial gene transcription can be accounted for by the binding of Btcd or H‐NS to a curved DNA sequence near a promoter. A few mammalian proteins have been shown to substitute for their Escherichia prototypes involved in DNA and RNA transactions. The efficiency of Btcd protein in substituting for H‐NS in Escherichia suggests its possible involvement in regulating gene expression in mouse cells.