Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding

Author:

Yang Min,Chen Xiao-ping,Militello Kevin,Hoffman Robert,Fernandez Bruce,Baumann Chris,Gollnick Paul

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference52 articles.

1. Requirements for transformation in Bacillus subtilis;Anagnostopoulos;J. Bacteriol.,1961

2. 11-Fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis;Antson;J. Mol. Biol.,1994

3. The structure of trp RNA-binding attenuation protein;Antson;Nature,1995

4. TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts;Babitzke;J. Biol. Chem.,1994

5. TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a toroid-shaped molecule that binds transcripts containing GAG or UAG repeats separated by two nucleotides;Babitzke;Proc. Natl Acad. Sci. USA.,1995

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