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72 residues of gal repressor fused to beta‐galactosidase repress the gal operon of E. coli.
Author(s) -
WilckenBergmann B.,
Koenen M.,
Griesser H.W.,
MüllerHill B.
Publication year - 1983
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.1460-2075.1983.tb01580.x
Subject(s) - operon , biology , repressor , physics , microbiology and biotechnology , genetics , escherichia coli , gene , gene expression
An active gene has been constructed which produces a chimera consisting of the N‐terminal domain of the gal repressor and all but the first five residues of beta‐galactosidase. Seventy two residues of gal repressor fused to beta‐galactosidase as tetrameric core are sufficient to repress the gal operon in vivo and to bind to the gal operator in vitro.