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

The trp RNA-binding attenuation protein of Bacillus subtilis, TRAP, regulates both transcription and translation by binding to specific transcript sequences. The optimal transcript sequences required for TRAP binding were determined by measuring complex formation between purified TRAP protein and sy...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 92; no. 17; pp. 7916 - 7920
Main Authors Babitzke, Paul, Bear, David G., Yanofsky, Charles
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 15.08.1995
National Acad Sciences
Subjects
Acetates
Bacillus subtilis
Bacillus subtilis - genetics
Bacillus subtilis - metabolism
Bacterial Proteins
Base Sequence
Binding Sites
Genes, Bacterial
Kinetics
Microsatellite repeats
Molecular Sequence Data
Molecules
Nucleic Acid Conformation
Nucleotides
Oligomers
Operon
Operons
Plasmids
Protein Conformation
Repetitive Sequences, Nucleic Acid
RNA
RNA, Bacterial - biosynthesis
RNA, Bacterial - chemistry
RNA-Binding Proteins - metabolism
RNA-Binding Proteins - ultrastructure
Terminator Regions, Genetic
Toroids
Transcription Factors - metabolism
Transcription Factors - ultrastructure
Transcription, Genetic
Transcriptional regulatory elements
Tryptophan - biosynthesis
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Summary:The trp RNA-binding attenuation protein of Bacillus subtilis, TRAP, regulates both transcription and translation by binding to specific transcript sequences. The optimal transcript sequences required for TRAP binding were determined by measuring complex formation between purified TRAP protein and synthetic RNAs. RNAs were tested that contained repeats of different trinucleotide sequences, with differing spacing between the repeats. A transcript containing GAG repeats separated by two-nucleotide spacers was bound most tightly. In addition, transmission electron microscopy was used to examine the structure of TRAP and the TRAP-transcript complex. TRAP was observed to be a toroid-shaped oligomer when free or when bound to either a natural or a synthetic RNA.
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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.92.17.7916