Solution structure of domain 1.1 of the σ
| Autor: | Milan, Zachrdla, Petr, Padrta, Alžbeta, Rabatinová, Hana, Šanderová, Ivan, Barvík, Libor, Krásný, Lukáš, Žídek |
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| Rok vydání: | 2017 |
| Předmět: |
DNA
Bacterial Models Molecular Carbon Isotopes Protein Folding Binding Sites Nitrogen Isotopes Protein Conformation Protein Stability Sigma Factor DNA-Directed RNA Polymerases Peptide Fragments Recombinant Proteins enzymes and coenzymes (carbohydrates) Protein Subunits Bacterial Proteins Structural Homology Protein Protein Structure and Folding bacteria Nucleic Acid Conformation Protein Interaction Domains and Motifs Thermotoga maritima Amino Acid Sequence Sequence Alignment Conserved Sequence Bacillus subtilis |
| Zdroj: | The Journal of biological chemistry. 292(28) |
| ISSN: | 1083-351X |
| Popis: | Bacterial RNA polymerase (RNAP) requires σ factors to recognize promoter sequences. Domain 1.1 of primary σ factors (σ1.1) prevents their binding to promoter DNA in the absence of RNAP, and when in complex with RNAP, it occupies the DNA-binding channel of RNAP. Currently, two 3D structures of σ1.1 are available: from Escherichia coli in complex with RNAP and from T. maritima solved free in solution. However, these two structures significantly differ, and it is unclear whether this difference is due to an altered conformation upon RNAP binding or to differences in intrinsic properties between the proteins from these two distantly related species. Here, we report the solution structure of σ1.1 from the Gram-positive bacterium Bacillus subtilis. We found that B. subtilis σ1.1 is highly compact because of additional stabilization not present in σ1.1 from the other two species and that it is more similar to E. coli σ1.1. Moreover, modeling studies suggested that B. subtilis σ1.1 requires minimal conformational changes for accommodating RNAP in the DNA channel, whereas T. maritima σ1.1 must be rearranged to fit therein. Thus, the mesophilic species B. subtilis and E. coli share the same σ1.1 fold, whereas the fold of σ1.1 from the thermophile T. maritima is distinctly different. Finally, we describe an intriguing similarity between σ1.1 and δ, an RNAP-associated protein in B. subtilis, bearing implications for the so-far unknown binding site of δ on RNAP. In conclusion, our results shed light on the conformational changes of σ1.1 required for its accommodation within bacterial RNAP. |
| Databáze: | OpenAIRE |
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