Disassembly intermediates of RbsD protein remain oligomeric despite the loss of an intact secondary structure

Science in China, Series C: Life Sciences

Volumn 52, Issue 11, 2009, Pages 997-1002

  Feng, Yong Jun ^a   Zhang, Meng ^b   Hu, Ming Xi ^a   Zheng, Jie ^a   Jiao, Wang Wang ^b   Chang, Zeng Yi ^b  

^a BEIJING INSTITUTE OF TECHNOLOGY   (China)

^b PEKING UNIVERSITY   (China)

Author keywords

Oligomeric intermediate; Oligomeric protein; RbsD; Reassembly; Refolding

Indexed keywords

ESCHERICHIA COLI PROTEIN; PROTEIN SUBUNIT; RBSD PROTEIN, E COLI; UREA;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; MOLECULAR GENETICS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

CIRCULAR DICHROISM; ESCHERICHIA COLI PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; UREA;

ESCHERICHIA COLI;

EID: 73249133405     PISSN: 10069305     EISSN: 18622798     Source Type: Journal    
DOI: 10.1007/s11427-009-0141-1     Document Type: Article

References (27)

1. Anfinsen C B. Principles that govern the folding of polypeptide chains. Science, 1973, 181: 223-230.
2. Gloss L M, Matthews C R. Mechanism of folding of the dimeric core domain of Escherichia coli Trp repressor: A nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry, 1998, 37: 15990-15999.
3. Doyle S M, Braswell E H, Teschke C M. SecA folds via a dimeric intermediate. Biochemistry, 2000, 39: 11667-11676.
4. Milla M E, Sauer R T. P22 Arc repressor: Folding kinetics of a single-domain, dimeric protein. Biochemistry, 1994, 33: 1125-1133.
5. Srivastava A K, Sauer R T. Evidence for partial secondary structure formation in the transition state for arc repressor refolding and dimerization. Biochemistry, 2000, 39: 8308-8314.
6. Jones S, Thornton J M. Principles of protein-protein interactions. Proc Natl Acad Sci USA, 1996, 93: 13-20.
7. Ryu K S, Kim C, Kim I, et al. NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration. J Biol Chem, 2004, 279: 25544-25548.
8. Kim M S, Shin J, Lee W, et al. Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture. J Biol Chem, 2003, 278: 28173-28180.
9. Feng Y, Jiao W, Chang Z, et al. Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein. Protein Sci, 2006, 15: 1441-1448.
10. Yamaoka T, Yamashita K, Itakura M. Determination of the number and relative molecular mass of subunits in an oligomeric protein by two-dimensional electrophoresis. J Chromatog, 1993, 630: 345-351.
11. Feng X, Huang S, Chang Z, et al. The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein Hsp16. 3 occurs via a stepwise mechanism. Biochem J, 2002, 363: 329-334.
12. Creighton T E. Detection of folding intermediates using urea-gradient electrophoresis. Methods Enzymol, 1986, 131: 156-172.
13. Goldenberg D P, Creighton T E. Gel electrophoresis in studies of protein conformation and folding. Anal Biochem, 1984, 138: 1-18.
14. Abulimiti A, Fu X, Chang Z, et al. Mycobacterium tuberculosis Hsp16. 3 nonamers are assembled and re-assembled via trimer and hexamer intermediates. J Mol Biol, 2003, 326: 1013-1023.
15. Jaenicke R. Protein folding: local structures, domains, subunits, and assemblies. Biochemistry, 1991, 30: 3147-3161.
16. Jaenicke R, Lilie H. Folding and association of oligomeric and multimeric proteins. Adv Protein Chem, 2000, 53: 329-401.
17. Jaenicke R, Rudolph R. Refolding and association of oligomeric proteins. Methods Enzymol, 1986, 131: 218-250.
18. Hong W, Jiao W, Chang Z, et al. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem, 2005, 280: 27029-27034.
19. Ziegler M M, Goldberg M E, Chaffotte A F, et al. Refolding of luciferase subunits from urea and assembly of the active heterodimer: Evidence for folding intermediates that precede and follow the dimerization step on the pathway to the active form of the enzyme. J Biol Chem, 1993, 268: 10760-10765.
20. Harpel P C, Cooper N R. Studies on human plasma C1 inactivator-enzyme interactions. I. Mechanisms of interaction with C1s, plasmin, and trypsin. J Clin Invest, 1975, 55: 593-604.
21. Moroi M, Yamasaki M. Mechanism of interaction of bovine trypsin with human alpha1-antitrypsin. Biochim Biophys Acta, 1974, 359: 130-141.
22. Travis J, Salvesen G S. Human plasma proteinase inhibitors. Annu Rev Biochem, 1983, 52: 655-709.
23. Perona J J, Tsu C A, Craik C S, et al. Crystal structure of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI. J Mol Biol, 1993, 230: 919-933.
24. Helland R, Leiros I, Berglund G I, et al. The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur J Biochem, 1998, 256: 317-324.
25. Berg J M, Tymoczko J L, Stryer L. Regulatory strategies: Enzymes and hemoglobin. In Biochemistry, 5th ed. (eds. J. M. Berg et al.), p. 283. W. H. New York: Freeman and Company. 2002.
26. Levy Y, Wolynes P G, Onuchic J N. Protein topology determines binding mechanism. Proc Natl Acad Sci USA, 2004, 101: 511-516.
27. Rousseau F, Schymkowitz J W H, Itzhaki L S. The unfolding story of three-dimensional domain swapping. Structure (London), 2003, 11, 243-251.