RNA-structural mimicry in Escherichia coli ribosomal protein L4-dependent regulation of the S10 operon Journal Article
| Authors: | Stelzl, U.; Zengel, J. M.; Tovbina, M.; Walker, M.; Nierhaus, K. H.; Lindahl, L.; Patel, D. J. |
| Article Title: | RNA-structural mimicry in Escherichia coli ribosomal protein L4-dependent regulation of the S10 operon |
| Abstract: | Ribosomal protein L4 regulates the 11-gene S10 operon in Escherichia coli by acting, in concert with transcription factor NusA, to cause premature transcription termination at a Rho-independent termination site in the leader sequence. This process presumably involves L4 interaction with the leader mRNA. Here, we report direct, specific, and independent binding of ribosomal protein L4 to the S10 mRNA leader in vitro. Most of the binding energy is contributed by a small hairpin structure within the leader region, but a 64-nucleotide sequence is required for the bona fide interaction. Binding to the S10 leader mRNA is competed by the 23 S rRNA L4 binding site. Although the secondary structures of the mRNA and rRNA binding sites appear different, phosphorothioate footprinting of the L4-RNA complexes reveals close structural similarity in three dimensions. Mutational analysis of the mRNA binding site is compatible with the structural model. In vitro binding of L4 induces structural changes of the S10 leader RNA, providing a first clue for how protein L4 may provoke transcription termination. |
| Keywords: | unclassified drug; nonhuman; proteins; genes; protein binding; transcription factor; transcription, genetic; dose-response relationship, drug; mutational analysis; rna; amino acid sequence; molecular sequence data; sequence homology, amino acid; rna, messenger; nucleotide sequence; escherichia coli; transcription; base sequence; gene control; models, molecular; binding sites; molecular structure; dna mutational analysis; nucleic acid conformation; rna structure; ribosome rna; biochemistry; protein structure, secondary; rna binding; ribosomal proteins; ribosome protein; 5' untranslated regions; phylogeny; iodine; gene expression regulation, enzymologic; operon; transcription termination; escherichia coli protein; binding, competitive; prokaryota; molecular mimicry; phosphorothioic acid; priority journal; article; ribosome protein l4; transcription factor nusa; collodion; rna, ribosomal, 23s |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 278 |
| Issue: | 30 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2003-07-25 |
| Start Page: | 28237 |
| End Page: | 28245 |
| Language: | English |
| DOI: | 10.1074/jbc.M302651200 |
| PUBMED: | 12738792 |
| PROVIDER: | scopus |
| PMCID: | PMC4692380 |
| DOI/URL: | |
| Notes: | Export Date: 12 September 2014 -- Source: Scopus |
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