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
Open Access
- 1 June 1994
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (24) , 16597-16604
- https://doi.org/10.1016/s0021-9258(19)89431-0
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho.Proceedings of the National Academy of Sciences, 1993
- MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.Proceedings of the National Academy of Sciences, 1993
- Assessing the multimeric states of proteins: Studies using laser desorption mass spectrometryJournal of Mass Spectrometry, 1991
- Com, the phage Mu mom translational activator, is a zinc-binding protein that binds specifically to its cognate mRNA.Proceedings of the National Academy of Sciences, 1991
- Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA II. Physical chemical studiesJournal of Molecular Biology, 1991
- Translational stimulation: RNA sequence and structure requirements for binding of Com proteinCell, 1991
- Rapid, sensitive analysis of protein mixtures by mass spectrometry.Proceedings of the National Academy of Sciences, 1990
- Interactions of Escherichia coli transcription termination factor rho with RNA: I. Binding stoichiometries and free energiesJournal of Molecular Biology, 1988
- Secondary structure of the circular form of the Tetrahymena rRNA intervening sequence: a technique for RNA structure analysis using chemical probes and reverse transcriptase.Proceedings of the National Academy of Sciences, 1985
- Improved Estimation of Secondary Structure in Ribonucleic AcidsNature New Biology, 1973