The anti-termination protein, HutP, regulates the gene expression of the hut (histidine utilization) operon of Bacillus subtilis, by destabilizing the hut terminator RNA located upstream of the coding region encoding L-histidine degradation enzymes. On the basis of biochemical, in vivo and X-ray structural analyses, we now report that HutP uses its dual RNA-binding surfaces to access two XAG-rich regions (sites I and II) within the terminator RNA to mediate the destabilization process. In this process, HutP initiates destabilization at the 5′-end of its mRNA by binding to the first XAG-rich region (site I) and then accesses the second XAG-rich region (site II), located downstream of the stable G-C-rich segment of the terminator stem. By this action, HutP appears to disrupt the G-C-rich terminator stem, and thus prevents premature termination of transcription in the RNA segment preceding the regions encoding for the histidine degradation enzymes. © 2008 The Author(s).
CITATION STYLE
Gopinath, S. C. B., Balasundaresan, D., Kumarevel, T., Misono, T. S., Mizuno, H., & Kumar, P. K. R. (2008). Insights into anti-termination regulation of the hut operon in Bacillus subtilis: Importance of the dual RNA-binding surfaces of HutP. Nucleic Acids Research, 36(10), 3463–3473. https://doi.org/10.1093/nar/gkn199
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