Folding of an isolated ribonuclease H core fragment

Protein Science

Volumn 8, Issue 11, 1999, Pages 2251-2257

  Chamberlain, Aaron K ^a   Fischer, Kael F ^a   Reardon, Deirdre ^a   Handel, Tracy M ^a   Marqusee, Susan ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b 229 Stanley Hall ^*  (United States)

Author keywords

Protein folding; Protein fragments; Ribonuclease H; Subdomain

Indexed keywords

HYDROGEN; RIBONUCLEASE H;

ARTICLE; CRYSTAL STRUCTURE; ESCHERICHIA COLI; ION EXCHANGE; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032698756     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.11.2251     Document Type: Article

References (35)

1. These authors contributed equally to this work. Azuaga AI, Conejero-Lara F, Rivas G, De Filippis V, Fontana, A, Mateo PL. 1995. The thermodynamics of association and unfolding of the 205-316 C-terminal fragment of thermolysin. Biochim Biophys Acta 1252:95-102.
2. Bai Y, Milne JS, Mayne L, Englander SW. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins 17:75-86.
3. Bax A, Ikura M, Kay LE, Torchia DA, Tschudin R. 1990. Comparison of different modes of 2-dimensional reverse-correlation NMR for the study of proteins. J Magn Reson 86:304-318.
4. Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping: A mechanism for oligomer assembly. Protein Sci 4:2455-2468.
5. Bowie JU, Sauer RT. 1989. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28:7139-7143.
6. Brown JE, Klee WA. 1969. Conformational studies of a series of overlapping peptides from ribonuclease and their relationship to the protein structure. Biochemistry 8:2876-2879.
7. Chamberlain AK, Handel TM, Marqusee S. 1996. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nat Struct Biol 3:782-787.
8. Chen H, Hughes DD, Chan T-A, Sedat JW, Agard DA. 1996. IVE (Image Visualization Environment): A software platform for all three-dimensional microscopy applications. J Struct Biol 116:56-60.
9. Conejero-Lara F, Mateo PL. 1996. Presence of a slow dimerization equilibrium on the thermal unfolding of the 205-316 thermolysin fragment at neutral pH. Biochemistry 35:3477-3486.
10. Constans AJ, Mayer MR, Sukits SF, Lecomte JT. 1998. A test of the relationship between sequence and structure in proteins: Excision of the heme binding site in apocytochrome b5. Protein Sci 7:1983-1993.
11. Dabora JM, Marqusee S. 1994. Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state. Protein Sci 3:1401-1408.
12. Dabora JM, Pelton JG, Marqusee S. 1996. Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry 35:11951-11958.
13. De Sanctis G, Ascoli F, Brunori M. 1994. Folding of apominimyoglobin. Proc Natl Acad Sci USA 91:11507-11511.
14. Edelhoch H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
15. Englander S, Sosnick T, Englander J, Mayne L. 1996. Mechanisms and uses of hydrogen exchange. Curr Opin Struct Biol 6:18-23.
16. Gegg CV, Bowers KE, Matthews CR. 1997. Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Sci 6:1885-1892.
17. Goedken ER, Raschke TM, Marqusee S. 1997. Importance of the C-terminal helix to the stability and enzymatic activity of Escherichia coli ribonuclease H. Biochemistry 36:7256-7263.
18. Grzesiek S, Bax A. 1992a. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114:6291-6293.
19. Grzesiek S, Bax A. 1992b. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J Magn Reson 99:201-207.
20. Katayanagi K, Miyagawa M, Matsushima M, Ishikawa M, Kanaya S, Nakamura H, Ikehara M, Matsuzaki T, Morikawa K. 1992. Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution. J Mol Biol 223:1029-1052.
21. 1H 2D NMR spectra by interactive computer graphics. J Magn Reson 84:627-633.
22. Llinás M, Marqusee S. 1998. Subdomain interactions as a determinant in the folding and stability of T4 lysozyme. Protein Sci 7:96-104.
23. McKnight CJ, Matsudaira PT, Kim PS. 1997. NMR structure of the 35-residue villin headpiece subdomain. Nat Struct Biol 4:180-184.
24. Oas T, Kim P. 1988. A peptide model of a protein folding intermediate. Nature 336:42-48.
25. Peng ZY, Kim PS. 1994. A protein dissection study of a molten globule. Biochemistry 33:2136-2141.
26. Raschke TM, Marqusee S. 1997. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat Struct Biol 4:298-304.
27. Rico M, Jimenez MA, Gonzalez C, De Filippis V, Fontana A. 1994. NMR solution structure of the C-terminal fragment 255-316 of thermolysin: A dimer formed by subunits having the native structure. Biochemistry 33: 14834-14847.
28. Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
29. Schlunegger MP, Bennett MJ, Eisenberg D. 1997. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly. In: Richards FM, Eisenberg DS, Kim PS, eds. Advances in protein chemistry. San Diego: Academic Press. pp 61-122.
30. Staley JP, Kim PS. 1990. Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor. Nature 344:685-688.
31. Taniuchi H, Anfinsen CB. 1969. An experimental approach to the study of the folding of staphylococcal nuclease. J Biol Chem 244:3864-3875.
32. Tasayco ML, Carey J. 1992. Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor. Science 255:594-597.
33. Tasayco ML, Chao K. 1995. NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation. Proteins 22:41-44.
34. 13C chemical-shift data. J Biomol NMR 4:171-180.
35. Yang JJ, Pikeathly M, Radford SE. 1994. Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme. Biochemistry 33:7345-7353.