Definition
Genomic studies are providing researchers with a potentially complete list of the molecular components present in living systems. It is now obvious that several metal ions are essential to life. More specifically, biological macromolecules (proteins and nucleic acids) that require metal ions to perform their physiological functions are widespread in all organisms. Here, we explored the importance and involvement of one of the alkali earth metals, barium, in the biological system. Based on structural and functional analyses, we clearly demonstrated how the divalent metal ions produce the structural rearrangements that are required for hut mRNA recognition. The applications and health risks of barium metal ions are also discussed.
General Background on Barium Metal
The chemical element barium is the 56th element in the chemical periodic table with the symbol of Ba...
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Antson AA, Dodson EJ, Dodson G, Greaves RB, Chen XP, Gollnick P (1999) Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. Nature 401:235–242
Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P (1995) The structure of trp RNA-binding attenuation protein. Nature 374:693–700
Barium (2001) In wikipedia, the free encyclopedia. Retrieved 20 Apr 2011, from http://en.wikipedia.org/wiki/Barium
Berman HM, Battistuz T, Bhat TN, Bluhm WF, Bourne PE, Burkhardt K, Feng Z, Gilliland GL, Iype L, Jain S, Fagan P, Marvin J, Padilla D, Ravichandran V, Schneider B, Thanki N, Weissig H, Westbrook JD, Zardecki C (2002) The protein data bank. Acta Crystallogr D Biol Crystallogr 58:899–907
Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE (2000) The protein data bank. Nucleic Acids Res. 28:235–242
Essen L-O, Perisic O, Lynch DE, Katan M, Williams RL (1997) A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-δ1. Biochemistry 36:2753–2762
Gollnick P, Babitzke P (2002) Transcription attenuation. Biochim Biophys Acta 1577:240–250
Gopinath SCB, Balasubramanian D, Kumarevel TS, Misono TS, Mizuno H, Kumar PKR (2008) Insights into anti-termination regulation of the hut operon in Bacillus subtilis: importance of the dual RNA-binding surfaces of HutP. Nucleic Acids Res 36:3463–3473
Herzfeld J, Griffin RG, Haberkorn RA (1978) 31P chemical-shift tensors in barium diethyl phosphate and urea-phosphoric acid: model compounds for phospholipid head-group studies. Biochemistry 17:2711–2718
Kumar PKR, Kumarevel TS, Mizuno H (2006) Structural basis of HutP-mediated transcription anti-termination. Curr Opin Struct Biol 16:18–26
Kumarevel TS (2007) Structural insights of HutP-mediated regulation of transcription of the hut operon in Bacillus subtilis. Biophys Chem 128:1–12
Kumarevel TS, Fujimoto Z, Padmanabhan B, Oda M, Nishikawa S, Mizuno H, Kumar PKR (2002) Crystallization and preliminary X-ray diffraction studies of HutP protein: an RNA-binding protein that regulates the transcription of hut operon in Bacillus subtilis. J Struct Biol 138:237–240
Kumarevel TS, Mizuno H, Kumar PKR (2003) Allosteric activation of HutP protein, that regulates transcription of hut operon in Bacillus subtilis, mediated by various analogs of histidine. Nucleic Acids Res Suppl 3:199–200
Kumarevel TS, Fujimoto Z, Karthe P, Oda M, Mizuno H, Kumar PKR (2004a) Crystal structure of activated HutP; an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis. Structure 12:1269–1280
Kumarevel TS, Fujimoto Z, Mizuno H, Kumar PKR (2004b) Crystallization and preliminary X-ray diffraction studies of the metal-ion-mediated ternary complex of the HutP protein with L-histidine and its cognate RNA. BBA- Prot Proteomics 1702:125–128
Kumarevel TS, Gopinath SCB, Nishikawa S, Mizuno H, Kumar PKR (2004c) Identification of important chemical groups of the hut mRNA for HutP interactions that regulate the hut operon in Bacillus subtilis. Nucleic Acids Res 32:3904–3912
Kumarevel TS, Mizuno H, Kumar PKR (2005a) Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand. Nature 434:183–191
Kumarevel TS, Mizuno H, Kumar PKR (2005b) Characterization of the metal ion binding site in the anti-terminator protein, HutP, of Bacillus subtilis. Nucleic Acids Res 33:5494–5502
Oda M, Katagai T, Tomura D, Shoun H, Hoshino T, Furukawa K (1992) Analysis of the transcriptional activity of the hut promoter in Bacillus subtilis and identification of a cis-acting regulatory region associated with catabolite repression downstream from the site of transcription. Mol Microbiol 6:2573–2582
Oda M, Kobayashi N, Ito A, Kurusu Y, Taira K (2000) cis-acting regulatory sequences for antitermination in the transcript of the Bacillus subtilis hut operon and histidine-dependent binding of HutP to the transcript containing the regulatory sequences. Mol Microbiol 35:1244–1254
Snyder S, Kim D, McIntosh TJ (1999) Lipopolysaccharide Bilayer structure: effect of chemotype, core mutations, divalent cations, and temperature. Biochemistry 38:10758–10767
Winter M, The periodic table on the web “WebElements™.” Source: WebElements http://www.webelements.com/
Yanofsky C (2000) Transcription attenuation: once viewed as a novel regulatory strategy. J Bacteriol 182:1–8
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media New York
About this entry
Cite this entry
Kumarevel, T. (2013). Barium and Protein–RNA Interactions. In: Kretsinger, R.H., Uversky, V.N., Permyakov, E.A. (eds) Encyclopedia of Metalloproteins. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1533-6_169
Download citation
DOI: https://doi.org/10.1007/978-1-4614-1533-6_169
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-1532-9
Online ISBN: 978-1-4614-1533-6
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences