Role of the N-terminal region and of β-sheet residue Thr29 on the activity of ω2 global regulator from the broad-host range Streptococcus pyogenes plasmid pSM19035

Biological Chemistry

Volumn 386, Issue 9, 2005, Pages 881-894

  Welfle, Karin ^a   Pratto, Florencia ^b   Misselwitz, Rolf ^a   Behlke, Joachim ^a   Alonso, Juan C ^b   Welfle, Heinz ^a  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

Author keywords

MetJ Arc superfamily; Protein folding; Protein DNA interaction; Thermodynamics; Transcriptional repressor

Indexed keywords

ALANINE; BACTERIAL DNA; DIMER; REGULATOR PROTEIN; THREONINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL STRAIN; BETA SHEET; BINDING AFFINITY; BINDING SITE; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MICROARRAY; PROTEIN STABILITY; PROTEIN VARIANT; STREPTOCOCCUS PYOGENES; THERMODYNAMICS; WILD TYPE;

BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; DNA FOOTPRINTING; DNA, BACTERIAL; DNA-BINDING PROTEINS; MODELS, MOLECULAR; OPERATOR REGIONS (GENETICS); PLASMIDS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; REPRESSOR PROTEINS; STREPTOCOCCUS PYOGENES; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; THREONINE; UREA;

STREPTOCOCCUS PYOGENES;

EID: 26844571814     PISSN: 14316730     EISSN: 14316730     Source Type: Journal    
DOI: 10.1515/BC.2005.103     Document Type: Article

References (33)

1. Acebo, P., Garcia de Lacoba, M., Rivas, G., Andreu, J.M., Espinosa, M., and del Solar, G. (1998). Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and β-sheet DNA binding proteins. Proteins 32, 248-261.
2. Blanco, A.G., Sola, M., Gomis-Ruth, F.X., and Coll, M. (2002). Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure (Camb.) 10, 701-713.
3. Bloomfield, V.A., Crothers, D.M., and Tinoco, I.J. (1999). Electronic and Vibrational Spectroscopy (Sausalito, CA, USA: University Science Books).
4. Brown, B.M., Milla, M.E., Smith, T.L., and Sauer, R.T. (1994). Scanning mutagenesis of the Arc repressor as a functional probe of operator recognition. Nat. Struct. Biol. 1, 164-168.
5. Connor, F., Cary, P.D., Read, C.M.P., Preston, N.S., Driscoll, P.C., Denny, P., Crane-Robinson, C., and Ashworth, A. (1994). DNA binding and bending properties of the post-meiotically expressed Sry-related protein Sox-5. Nucleic Acids Res. 22, 3339-3346.
6. de la Hoz, A.B., Ayora, S., Sitkiewicz, I., Fernandez, S., Pankiewicz, R., Alonso, J.C., and Ceglowski, P. (2000). Plasmid copy-number control and better-than-random segregation genes of pSM19035 share a common regulator. Proc. Natl. Acad. Sci. USA 97, 728-733.
7. de la Hoz, A.B., Pratto, F., Misselwitz, R., Speck, C., Weihofen, W., Welfle, K., Saenger, W., Welfle, H., and Alonso, J.C. (2004). Recognition of DNA by ω protein from the broad-host range Streptococcus pyogenes plasmid pSM19035: analysis of binding to operator DNA with one to four heptad repeats. Nucleic Acids Res. 32, 3136-3147.
8. Dominy, B.N., Perl, D., Schmid, F.X., and Brooks, C.L. III (2002). The effects of ionic strength on protein stability: the cold shock protein family. J. Mol. Biol. 319, 541-554.
9. Dostál, L., Misselwitz, R., Laettig, S., Alonso, J.C., and Welfle, H. (2003). Raman spectroscopy of regulatory protein omega from Streptococcus pyogenes plasmid pSM19035 and complexes with operator DNA. Spectroscopy 17, 435-445.
10. Golovanov, A.P., Barilla, D., Golovanova, M., Hayes, F., and Lian, L.Y. (2003). ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. Mol. Microbiol. 50, 1141-1153.
11. Gomis-Ruth, F.X., Sola, M., Acebo, P., Parraga, A., Guasch, A., Eritja, R., Gonzalez, A., Espinosa, M., del Solar, G., and Coll, M. (1998). The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator. EMBO J. 17, 7404-7415.
12. Gupta, V., Peterson, C.B., Dice, L.T., Uchiki, T., Racca, J., Guo, J.T., Xu, Y., Hettich, R., Zhao, X., Rothstein, R., and Dealwis, C.G. (2004). Sml1p is a dimer in solution: characterization of denaturation and renaturation of recombinant Sml1p. Biochemistry 43, 8568-8578.
13. Johnson, W.C. Jr. (1990). Protein secondary structure and circular dichroism: a practical guide. Proteins Struct. Funct. Genet. 7, 205-214.
14. Kalivoda, K.A., Steenbergen, S.M., Vimr, E.R., and Plumbridge, J. (2003). Regulation of sialic acid catabolism by the DNA binding protein NanR in Escherichia coli. J. Bacteriol. 185, 4806-4815.
15. Misselwitz, R., de la Hoz, A.B., Ayora, S., Welfle, K., Behlke, J., Murayama, K., Saenger, W., Alonso, J.C., and Welfle, H. (2001). Stability and DNA-binding properties of the ω regulator protein from the broad-host range Streptococcus pyogenes plasmid pSM19035. FEBS Lett. 505, 436-440.
16. Moller-Jensen, J., Borch, J., Dam, M., Jensen, R.B., Roepstorff, P., and Gerdes, K. (2003). Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism. Mol. Cell 12, 1477-1487.
17. Movileanu, L., Benevides, J.M., and Thomas Jr., G.J. (2002). Determination of base and backbone contributions to the thermodynamics of premelting and melting transitions in B DNA. Nucleic Acids Res. 30, 3767-3777.
18. Mueller, U., Perl, D., Schmid, F.X., and Heinemann, U. (2000). Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein. J. Mol. Biol. 297, 975-988.
19. Murayama, K., Orth, P., de la Hoz, A.B., Alonso, J.C., and Saenger, W. (2001). Crystal structure of ω transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 Å resolution. J. Mol. Biol. 314, 789-796.
20. Nagaich, A.K., Bhattacharyya, D., Brahmachari, S.K., and Bansal, M. (1994). CA/TG sequence at the 5′ end of oligo(A)-tracts strongly modulates DNA curvature. J. Biol. Chem. 269, 7824-7833.
21. Olins, D.E., Bryan, P.N., Harrington, R.E., Hill, W.E., and Olins, A.L. (1977). Conformational states of chromatin nu bodies induced by urea. Nucleic Acids Res. 4, 1911-1931.
22. Pace, C.N. and Scholtz, J.M. (1997). Measuring the conformational stability of a protein. In: Protein Structure: A Practical Approach, T.E. Creighton, ed. (Oxford, New York, Tokyo: IRL Press), pp. 299-321.
23. Park, Y.W. and Breslauer, K.J. (1991). A spectroscopic and calorimetric study of the melting behaviors of a 'bent' and a 'normal' DNA duplex: [d(GA4T4C)]2 versus [d(GT4A4C)]2. Proc. Natl. Acad. Sci. USA 88, 1551-1555.
24. Perl, D. and Schmid, F.X. (2001). Electrostatic stabilization of a thermophilic cold shock protein. J. Mol. Biol. 313, 343-357.
25. Ptashne, M. (1986). A Genetic Switch. Gene Control and Phage Lambda (Cambridge, UK: Cell Press/Blackwell Scientific Publications).
26. Ramstein, J., Hervouet, N., Coste, F., Zelwer, C., Oberto, J., and Castaing, B. (2003). Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure. J. Mol. Biol. 331, 101-121.
27. Raumann, B.E., Rould, M.A., Pabo, C.O., and Sauer, R.T. (1994). DNA recognition by β-sheets in the Arc repressor-operator crystal structure. Nature 367, 754-757.
28. Robinson, C.R., Rentzeperis, D., Silva, J.L., and Sauer, R.T. (1997). Formation of a denatured dimer limits the thermal stability of Arc repressor. J. Mol. Biol. 273, 692-700.
29. Schildbach, J.F., Karzai, A.W., Raumann, B.E., and Sauer, R.T. (1999). Origins of DNA-binding specificity: role of protein contacts with the DNA backbone. Proc. Natl. Acad. Sci. USA 96, 811-817.
30. Schreiter, E.R., Sintchak, M.D., Guo, Y., Chivers, P.T., Sauer, R.T., and Drennan, C.L. (2003). Crystal structure of the nickel-responsive transcription factor NikR. Nat. Struct. Biol. 10, 794-799.
31. Shortle, D. (1996). The denatured state (the other half of the folding reaction) and its role in protein stability. FASEB J. 10, 27-34.
32. Somers, W.S. and Phillips, S.E. (1992). Crystal structure of the met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by β-strands. Nature 359, 387-393.
33. Somers, W.S., Rafferty, J.B., Phillips, K., Strathdee, S., He, Y.Y., McNally, T., Manfield, I., Navratil, O., Old, I.G., Saint-Girons, I., et al. (1994). The Met repressor-operator complex: DNA recognition by β-strands. Ann. N.Y. Acad. Sci. 726, 105-117.