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Accession number;06A0382477
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| Title;Crystallographic Studies to Reveal Insights of HutP-mediated Transcription Anti-termination Mechanism |
| Author;
MIZUNO HIROSHI
(Necsofuto Vtcse)
KUMAREVEL THIRUMANANSERI
(Inst. Physical and Chemical Res., JPN)
KUMAR PENMETCHA K.R.
(Inst. Biological Resources and Functions, National Inst. Advanced Industrial Sci. and Technol., JPN)
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Journal Title;Journal of the Crystallographic Society of Japan
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Journal Code:G0232A
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ISSN:0369-4585
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VOL.48;NO.2;PAGE.153-159(2006)
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| Figure&Table&Reference;FIG.6, TBL.1, REF.14 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Anti-terminator proteins control gene expression by recognizing control signals on cognate mRNAs and preventing transcriptional termination. HutP of Bacillus subtilis regulates the hut operon by an anti-termination mechanism. Recently, crystal structures of HutP [apo-form of HutP, HutP-HBN (histidine analog), HutP-L-histidine-Mg'2+', and HutP-L-histidine-Mg'2+'-RNA] have been reported. These structures and functional studies on HutP showed how the protein undergoes conformational changes in response to two key components: L-histidine and Mg'2+' ions, before binding to the cognate terminator RNA. (author abst.) |
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