Sequence determinants of folding and stability for the P22 Arc repressor dimer

FASEB Journal

Volumn 10, Issue 1, 1996, Pages 42-48

  Sauer, Robert T ^a   Milla, Marcos E ^a,b   Waldburger, Carey D ^a   Brown, Bronwen M ^a,c   Schildbach, Joel F ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b GLAXOSMITHKLINE   (United States)

^c UNIVERSITY OF OREGON   (United States)

Author keywords

buried polar interactions; combinatorial mutagenesis; hydrophobic core; side chain information; transition state

Indexed keywords

REPRESSOR PROTEIN; VIRUS PROTEIN;

AMINO ACID SEQUENCE; BACTERIOPHAGE P22; CONFORMATIONAL TRANSITION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; REVIEW;

EID: 0030065958     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.1.8566546     Document Type: Review

References (21)

1. Susskind, M. M., and Youderian, P. (1983) Lambda II (Hendrix, R. W., Roberts, J. W., Stahl, F. W., and Weisberg, R. A., eds) pp. 347-364, Cold Spring Harbor Laboratory, New York
2. Vershon, A. K., Liao, S-M., McClure, W. R., and Sauer, R. T. (1987) Interaction of the bacteriophage P22 Arc repressor with operator DNA. J. Mol. Biol. 195, 323-331
3. Breg, J. N., van Opheusden, J. H. J., Burgering, M. J., Boelens, R., and Kaptein, R. (1990) Structure of Arc repressor in solution: evidence for a family of β-sheet DNA-binding proteins. Nature (London) 346, 586-589
4. Bonvin, A. M. J. J., Vis, H., Breg, J. N., Burgering, M. J- M., Boelens, R., and Kaptein, R. (1994) Nuclear magnetic resonance solution structure of the Arc repressor using relaxation matrix calculations. J. Mol. Biol. 236, 328-341
5. 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 (London) 367, 754-757
6. Bowie, J. U.,and Sauer, R.T. (1989a) Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28, 7139-7143
7. Milla, M. E., and Sauer, R. T. (1994) P22 Arc repressor: folding kinetics of a single domain, dimeric protein. Biochemistry 33, 1125-1133
8. Silva, J. L., Silveira, C. F., Corieia, A., Jr., and Pontes, L. (1992) Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of Arc repressor. J. Mol. Biol. 223, 545-555
9. 1H NMR spectroscpoy. Proc. Natl. Acad. Sci. USA 90, 1776-1780
10. Burgering, M. J., Hald, M., Boelens, R., Breg, J. N., and Kaptein, R. (1995) Hydrogen exchange studies of the Arc repressor. Biopolymers 35, 217-226
11. Milla, M. E., Brown, B. M., and Sauer, R. T. (1994) Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nature Struct. Biol. 1,518-523
12. Milla, M. E., Brown, B. M., Waldburger, C. D., and Sauer, R. T. (1995) P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry 34, 1394-13919
13. Vershon, A. K., Bowie, J. U., Karplus, T. M., and Sauer, R. T. (1986) Isolation and analysis of Arc repressor mutants: evidence for an unusual mechanism of DNA binding. Proteins: Struct. Funct. Genet. 1, 302-311
14. Schildbach, J. F., Milla, M. E., Jeffrey, P. D., Raumann, B. E., and Sauer, R. T. (1995) Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8. Biochemistry 34, 1405-1412
15. Milla, M. E., and Sauer, R. T. (1995) Critical side-chain interactions at a subunit interface in the Arc repressor dimer. Biochemistry 34, 3344-3351
16. Waldburger, C. D., Schildbach, J. F., and Sauei, R. T. (1995) Are buried salt bridges important for protein stability and conformational specificity. Nature Struct. Biol. 2,122-128
17. Hendsch, Z. S., and Tidor, B. (1994) Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Science 3, 211-226
18. Bowie, J. U., and Sauer, R. T. (1989b) Identifying determinants of folding and activity for a protein of unknown structure. Proc. Natl. Acad. Sci. USA 86, 2152-2156
19. Tanford, C. (1970) Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24,1-95
20. Fersht, A. R., Itzhaki, L. S., ElMasry, N. F., Matthews, J. M., and Otzen, D. E. (1994) Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl. Acad. Sci. USA 91, 10426-10429
21. Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 964-950