Positions of Trp Codons in the Leader Peptide-Coding Region of the at Operon Influence Anti-Trap Synthesis and trp Operon Expression in Bacillus licheniformis

• DOI: 10.1128/jb.01420-09
• Publication Date: 2010-01-09T02:57:25Z
• Authors: Anastasia Levitin; Charles Yanofsky
• Keywords: trp operon; Bacillus licheniformis; Peptide Biosynthesis

Tryptophan, phenylalanine, tyrosine, and several other metabolites are all synthesized from a common precursor, chorismic acid. Since tryptophan is product of an energetically expensive biosynthetic pathway, bacteria have developed sensing mechanisms to downregulate synthesis the enzymes formation when amino acid not needed. In Bacillus subtilis some Gram-positive bacteria, trp operon expression regulated by two proteins, TRAP (the tryptophan-activated RNA binding protein) AT anti-TRAP protein). activated bound tryptophan, increased upon accumulation uncharged tRNA(Trp). Tryptophan-activated binds leader RNA, generating terminator structure that promotes transcription termination. TRAP, inhibiting its ability. B. subtilis, upregulated both transcriptionally translationally in response this paper, we focus on explaining differences organization regulatory functions at operon's peptide-coding region, rtpLP, licheniformis. Our objective was correlate greater growth sensitivity licheniformis starvation with spacing three Trp codons region. findings suggest codon location rtpLP designed allow mild charged-tRNA(Trp) deficiency expose Shine-Dalgarno sequence start for protein, leading synthesis.