Defying stereotypes: The elusive search for a universal model of LysR-type regulation

Molecular Microbiology

Volumn 83, Issue 3, 2012, Pages 453-456

  Momany, Cory ^a   Neidle, Ellen L ^a  

^a UNIVERSITY OF GEORGIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APHB PROTEIN; BACTERIAL PROTEIN; LYSR TYPE TRANSCRIPTION REGULATOR PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; BACTERIAL VIRULENCE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DNA BINDING MOTIF; DNA SEQUENCE; MOLECULAR DYNAMICS; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; NOTE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; SEQUENCE ANALYSIS; VIBRIO CHOLERAE;

BACTERIAL PROTEINS; OXYGEN; TRANS-ACTIVATORS; VIBRIO CHOLERAE;

VIBRIO CHOLERAE;

EID: 84856039053     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07960.x     Document Type: Note

References (18)

1. Craven, S.H., Ezezika, O.C., Momany, C., and Neidle, E.L. (2008) LysR homologs in Acinetobacter: insights into a diverse and prevalent family of transcriptional regulators. In Acinetobacter Molecular Biology. Gerischer, U. (ed.). Norfolk: Caister Academic Press, pp. 163-202.
2. Craven, S.H., Ezezika, O.C., Haddad, S., Hall, R.A., Momany, C., and Neidle, E.L. (2009) Inducer responses of BenM, a LysR-type transcriptional regulator from Acinetobacter baylyi ADP1. Mol Microbiol 72: 881-894.
3. Devesse, L., Smirnova, I., Lonneborg, R., Kapp, U., Brzezinski, P., Leonard, G.A., and Dian, C. (2011) Crystal structures of DntR inducer binding domains in complex with salicylate offer insights into the activation of LysR-type transcriptional regulators. Mol Microbiol 81: 354-367.
4. Ezezika, O.C., Haddad, S., Neidle, E.L., and Momany, C. (2007a) Oligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this family. Acta Crystallograph Sect F Struct Biol Cryst Commun 63: 361-368.
5. Ezezika, O.C., Haddad, S., Clark, T.J., Neidle, E.L., and Momany, C. (2007b) Distinct effector-binding sites enable synergistic transcriptional activation by BenM, a LysR-type regulator. J Mol Biol 367: 616-629.
6. Henikoff, S., Haughn, G.W., Calvo, J.M., and Wallace, J.C. (1988) A large family of bacterial activator proteins. Proc Natl Acad Sci USA 85: 6602-6606.
7. Kovacikova, G., Lin, W., and Skorupski, K. (2004) Vibrio cholerae AphA uses a novel mechanism for virulence gene activation that involves interaction with the LysR-type regulator AphB at the tcpPH promoter. Mol Microbiol 53: 129-142.
8. Kovacikova, G., Lin, W., and Skorupski, K. (2010) The LysR-type virulence activator AphB regulates the expression of genes in Vibrio cholerae in response to low pH and anaerobiosis. J Bacteriol 192: 4181-4191.
9. Monferrer, D., Tralau, T., Kertesz, M.A., Dix, I., Sola, M., and Uson, I. (2010) Structural studies on the full-length LysR-type regulator TsaR from Comamonas testosteroni T-2 reveal a novel open conformation of the tetrameric LTTR fold. Mol Microbiol 75: 1199-1214.
10. Muraoka, S., Okumura, R., Ogawa, N., Nonaka, T., Miyashita, K., and Senda, T. (2003) Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend. J Mol Biol 328: 555-566.
11. Pareja, E., Pareja-Tobes, P., Manrique, M., Pareja-Tobes, E., Bonal, J., and Tobes, R. (2006) ExtraTrain: a database of extragenic regions and transcriptional information in prokaryotic organisms. BMC Microbiol 6: 29.
12. Pomposiello, P.J., Janes, B.K., and Bender, R.A. (1998) Two roles for the DNA recognition site of the Klebsiella aerogenes nitrogen assimilation control protein. J Bacteriol 180: 578-585.
13. Ruangprasert, A., Craven, S.H., Neidle, E.L., and Momany, C. (2010) Full-length structures of BenM and two variants reveal different oligomerization schemes for LysR-type transcriptional regulators. J Mol Biol 404: 568-586.
14. Sainsbury, S., Lane, L.A., Ren, J., Gilbert, R.J., Saunders, N.J., Robinson, C.V., etal. (2009) The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators. Nucleic Acids Res 37: 4545-4558.
15. Smirnova, I.A., Dian, C., Leonard, G.A., McSweeney, S., Birse, D., and Brzezinski, P. (2004) Development of a bacterial biosensor for nitrotoluenes: the crystal structure of the transcriptional regulator DntR. J Mol Biol 340: 405-418.
16. Taylor, J.L., De Silva, R.S., Kovacikova, G., Lin, W., Taylor, R.K., Skorupski, K., and Kull, F.J. (2012) The crystal structure of AphB, a virulence gene activator from Vibrio cholerae, reveals residues that influence its response to oxygen and pH. Mol Microbiol 83: 457-470.
17. Tyrrell, R., Verschueren, K.H., Dodson, E.J., Murshudov, G.N., Addy, C., and Wilkinson, A.J. (1997) The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement. Structure 5: 1017-1032.
18. Zhou, X., Lou, Z., Fu, S., Yang, A., Shen, H., Li, Z., etal. (2010) Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation. J Mol Biol 396: 1012-1024.