Assessment of substrate-stabilizing factors for DnaK on the folding of aggregation-prone proteins

Biochemical and Biophysical Research Communications

Volumn 373, Issue 1, 2008, Pages 74-79

  Ryu, Kisun ^a   Kim, Chul Woo ^a   Kim, Byung Hee ^a   Han, Kyoung Sim ^a   Kim, Kyun Hwan ^b   Choi, Seong Il ^a   Seong, Baik L ^a  

^a Yonsei University   (South Korea)

^b Department of Pharmacology   (South Korea)

Author keywords

Aggregation; DnaK; Hydrophobic interactions; Molecular chaperones; Substrate stabilization

Indexed keywords

HYBRID PROTEIN; PROTEIN DNAK;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; COVALENT BOND; ENZYME SUBSTRATE; GENE DELETION; GENE MUTATION; HUMAN; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN VARIANT; SOLUBILIZATION;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HYDROPHOBICITY; POINT MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SOLUBILITY;

EID: 45949111777     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.05.186     Document Type: Article

References (29)

1. Bukau B., and Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92 (1998) 351-366
2. Hartl F.U., and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002) 1852-1858
3. VorderwÜlbecke S., Kramer G., Merz F., Kurz T.A., Rauch T., Zachmann-Brand B., Bukau B., and Deuerling E. Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett. 559 (2004) 181-187
4. Kerner M.J., Naylor D.J., Ishihama Y., Maier T., Chang H.C., Stines A.P., Georgopoulos C., Frishman D., Hayer-Hartl M., Mann M., and Hartl F.U. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122 (2005) 209-220
5. Zhu X., Zhao X., Burkholder W.F., Gragerov A., Ogata C.M., Gottesman M.E., and Hendrickson W.A. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272 (1996) 1606-1614
6. Rüdiger S., Germeroth L., Schneider-Mergener J., and Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16 (1997) 1501-1507
7. Misselwitz B., Staeck O., and Rapoport T.A. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol. Cell 2 (1998) 593-603
8. Aoki K., Taguchi H., Shindo Y., Yoshida M., Ogasahara K., Yutani K., and Tanaka N. Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. J. Biol. Chem. 272 (1997) 32158-32162
9. Edwards K.L., Kueltzo L.A., Fisher M.T., and Middaugh C.R. Complex effects of molecular chaperones on the aggregation and refolding of fibroblast growth factor-1. Arch. Biochem. Biophys. 393 (2001) 14-21
10. Pappenberger G., Wilsher J.A., Roe S.M., Counsell D.J., Willison K.R., and Pearl L.H. Crystal structure of the CCTγ apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. J. Mol. Biol. 318 (2002) 1367-1379
11. Trombetta E.S., and Helenius A. Lectins as chaperones in glycoprotein folding. Curr. Opin. Struct. Biol. 8 (1998) 587-892
12. Lawrence M.S., Phillips K.J., and Liu D.R. Supercharging proteins can impart unusual resilience. J. Am. Chem. Soc. 129 (2007) 10110-10112
13. Otzen D.E., Kristensen O., and Oliveberg M. Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly. Proc. Natl. Acad. Sci. USA 97 (2000) 9907-9912
14. Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions. Proteins 41 (2000) 415-427
15. Zhang Y.B., Howitt J., McCorkle S., Lawrence P., Springer K., and Freimuth P. Protein aggregation during overexpression limited by peptide extensions with large net negative charge. Protein Expr. Purif. 36 (2004) 207-216
16. Su Y., Zou Z., Feng S., Zhou P., and Cao L. The acidity of protein fusion partners predominantly determines the efficacy to improve the solubility of the target proteins expressed in Escherichia coli. J. Biotechnol. 129 (2007) 373-382
17. Chiti F., Calamai M., Taddei N., Stefani M., Ramponi G., and Dobson C.M. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl. Acad. Sci. USA 99 (2002) 16419-16426
18. Høiberg-Nielsen R., Fuglsang C.C., Arleth L., and Westh P. Interrelationships of glycosylation and aggregation kinetics for Peniophora lycii phytase. Biochemistry 45 (2006) 5057-5066
19. Rajan R.S., Li T., Aras M., Sloey C., Sutherland W., Arai H., Briddell R., Kinstler O., Lueras A.M., Zhang Y., Yeghnazar H., Treuheit M., and Brems D.N. Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study. Protein Sci. 15 (2006) 1063-1075
20. Kim C.W., Han K.S., Ryu K.S., Kim B.H., Kim K.H., Choi S.I., and Seong B.L. N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers. Protein Sci. 16 (2007) 635-643
21. Castanie M.P., Berges H., Oreglia J., Prere M.F., and Fayet O. A set of pBR322-compatible plasmids allowing the testing of chaperone-assisted folding of proteins overexpressed in Escherichia coli. Anal. Biochem. 254 (1997) 150-152
22. Wall J.G., and Plückthun A. Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6 (1995) 507-516
23. Mayer M.P., Schröder H., Rüdiger S., Paal K., Laufen T., and Bukau B. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. 7 (2000) 586-593
24. Rüdiger S., Mayer M.P., Schneider-Mergener J., and Bukau B. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. J. Mol. Biol. 304 (2000) 245-251
25. Ellis R.J. Molecular chaperones. Opening and closing the Anfinsen cage. Curr. Biol. 4 (1994) 633-635
26. Agard D.A. To fold or not to fold. Science 260 (1993) 1903-1904
27. Nallamsetty S., and Waugh D.S. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Expr. Purif. 45 (2006) 175-182
28. van den Berg B., Ellis R.J., and Dobson C.M. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18 (1999) 6927-6933
29. Agashe V.R., Guha S., Chang H.C., Genevaux P., Hayer-Hartl M., Stemp M., Georgopoulos C., Hartl F.U., and Barral J.M. Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell 117 (2004) 199-209