Metal ion-dependent anti-termination of transcriptional regulation of ribonucleoprotein complexes

Biophysics Reviews
Penmetcha K R Kumar, Hiroshi Mizuno

Abstract

Anti-terminator proteins are frequently used by bacteria to sense a specific metabolite signal and direct RNA polymerase to either terminate or continue transcription of the genes downstream of an operon. One such protein is HutP, which binds to upstream cis-regulatory sequences to regulate expression of the histidine utilization (hut) operon in Bacillus subtilis. HutP must be activated by L-histidine and divalent metal ions before binding to hut mRNA; binding of activated HutP prevents termination of transcription. Thus, HutP appears to regulate the hut operon in a unique fashion in this class of regulatory proteins. To understand gene (hut operon) regulation by HutP, we performed several biochemical and structural studies. These studies reveal events in the regulatory mechanism, starting with the activation of HutP and ending with the unwinding of hut terminator RNA. In this review, we describe the unique regulatory mechanisms commonly used by many Bacillus species.

References

Nov 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·S Aymerich, M Steinmetz
Jan 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·P Babitzke, C Yanofsky
Dec 10, 1996·Proceedings of the National Academy of Sciences of the United States of America·Y LuR L Switzer
Sep 30, 2005·Nucleic Acids Research·Thirumananseri KumarevelPenmetcha K R Kumar
Aug 31, 2012·Microbiology and Molecular Biology Reviews : MMBR·Robert A Bender
Jun 12, 2013·Journal of Structural Biology·Balasundaresan DhakshnamoorthyPenmetcha K R Kumar

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Citations

May 19, 2019·Annual Review of Microbiology·Paul BabitzkeTony Romeo

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