Nihon Kessho Gakkaishi
Online ISSN : 1884-5576
Print ISSN : 0369-4585
ISSN-L : 0369-4585
Crystallographic Studies to Reveal Insights of HutP-mediated Transcription Antitermination Mechanism
Hiroshi MIZUNOThirumananseri KUMAREVELPenmetcha K. R. KUMAR
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JOURNAL FREE ACCESS

2006 Volume 48 Issue 2 Pages 153-159

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Abstract
Anti-terminator proteins control gene expression by recognizing control signals on cognate mRNAs and preventing transcriptional termination. HutP ofBacillus subtilisregulates thehutoperon by an anti-termination mechanism. Recently, crystal structures of HutP [apo-form of HutP, HutP-HBN (histidine analog), HutP-L-histidine-Mg2+, and HutP-L-histidine-Mg2+-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 Mg2+ions, before binding to the cognate terminator RNA.
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© The Crystallographic Society of Japan
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