Structural basis of HutP-mediated transcription anti-termination

Current Opinion in Structural Biology

Volumn 16, Issue 1, 2006, Pages 18-26

  Kumar, Penmetcha K R ^a   Kumarevel, Thirumananseri ^a,c   Mizuno, Hiroshi ^b  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b NEC CORPORATION   (Japan)

^c RIKEN HARIMA INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHEMICAL COMPOUND; HISTIDINE; HISTIDINE DERIVATIVE; MAGNESIUM ION; METAL ION; PROTEIN HUTP; RNA; UNCLASSIFIED DRUG;

COMPARATIVE STUDY; CRYSTAL STRUCTURE; GENE REARRANGEMENT; GENE STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; REVIEW; TRANSCRIPTION REGULATION;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; BASE SEQUENCE; HISTIDINE; MOLECULAR SEQUENCE DATA; OPERON; RNA-BINDING PROTEINS; TERMINATOR REGIONS, GENETIC; TRANSCRIPTION, GENETIC;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 32344431968     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.01.005     Document Type: Review

References (22)

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17. T.S. Kumarevel, Z. Fujimoto, B. Padmanabhan, M. Oda, S. Nishikawa, H. Mizuno, and P.K.R. Kumar 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 2002 237 240
18. T. Kumarevel, Z. Fujimoto, P. Karthe, M. Oda, H. Mizuno, and P.K.R. Kumar Crystal structure of activated HutP: an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis Structure 12 2004 1269 1280 The first reported crystal structure of HutP complexed with an l-histidine analog. The important chemical groups of l-histidine that enable HutP recognition of the cognate mRNA were identified. A minimal RNA motif containing three UAG motifs was suggested to be the core region for HutP binding.
19. T.S. Kumarevel, H. Mizuno, and P.K. Kumar 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 2003 199 200
20. 2+ ion in the complexes.
21. T.S. Kumarevel, S.C.B. Gopinath, S. Nishikawa, H. Mizuno, and P.K.R. Kumar Identification of important chemical groups of the hut mRNA for HutP interactions that regulate the hut operon in Bacillus subtilis Nucleic Acids Res 32 2004 3904 3912 The important chemical groups of the RNA within the UAG motif were identified and the 1:2 molar ratio (protein:RNA) of HutP-RNA binding was determined. Furthermore, Glu137 of HutP was proposed to be very important for the HutP-hut mRNA interaction.
22. T. Kumarevel, H. Mizuno, and P.K.R. Kumar Characterization of the metal ion binding site in the anti-terminator protein, HutP, of Bacillus subtilis Nucleic Acids Res 33 2005 5494 5502 This study showed that several different divalent metal ions can mediate the HutP protein-RNA interaction, but monovalent cations cannot. An efficient divalent metal ion binding pocket was identified.