PMID: 8955380Dec 1, 1996Paper

The linker region of AraC protein

Journal of Bacteriology
R J Eustance, Robert F Schleif

Abstract

AraC protein, a transcriptional regulator of the L-arabinose operon in Escherichia coli, is dimeric. Each monomer consists of a domain for DNA binding plus transcription activation and a domain for dimerization plus arabinose binding. These are connected to one another by a linker region of at least 5 amino acids. Here we have addressed the question of whether any of the amino acids in the linker region play active, specific, and crucial structural roles or whether these amino acids merely serve as passive spacers between the functional domains. We found that all but one of the linker amino acids can be changed to other amino acids individually and in small groups without substantially affecting the ability of AraC protein to activate transcription when arabinose is present. When, however, the entire linker region is replaced with linker sequences from other proteins, the functioning of AraC is impaired.

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Citations

Aug 16, 2011·Journal of Bacteriology·Jennifer Seedorff, Robert Schleif
May 30, 1998·Proceedings of the National Academy of Sciences of the United States of America·C R Robinson, R T Sauer
Dec 16, 2017·Applied Microbiology and Biotechnology·Chun-Li LiuTian-Wei Tan
Jan 29, 2000·Journal of Bacteriology·N KaldaluM Ustav
Oct 31, 2006·Journal of Bacteriology·Ana KolinSusan M Egan
Apr 11, 2021·FEMS Microbiology Reviews·Daniel Cortés-AvalosJ Antonio Ibarra
Jun 20, 1998·Journal of Molecular Biology·B SaviolaR F Schleif
Apr 5, 2001·Journal of Molecular Biology·M Wu, R Schleif
Jun 20, 1998·Journal of Molecular Biology·R R Seabold, R F Schleif
Dec 1, 2004·EcoSal Plus·Charles J Dorman
Dec 31, 1997·Microbiology and Molecular Biology Reviews : MMBR·M T GallegosJ L Ramos
Sep 20, 2000·Biochemistry·N LaRonde-LeBlanc, C Wolberger
Apr 18, 1997·Science·S M SoissonC Wolberger

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