YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3)

FEBS Letters

Volumn 586, Issue 7, 2012, Pages 1044-1048

  Ahn, Keum Young ^a   Park, Jin Seung ^a   Han, Kyung Yeon ^a,b   Song, Jong Am ^a   Lee, Jeewon ^a  

^a Korea University   (South Korea)

^b SAMSUNG Electronics   (South Korea)

Author keywords

BL21(DE3); Chaperone like protein; Heat shock; YrhB

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; CHAPERONE; HEAT SHOCK PROTEIN; HYBRID PROTEIN; MONOMER; RIBONUCLEOTIDE SYNTHASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE; YRHB PROTEIN;

ARTICLE; CELL INCLUSION; CONTROLLED STUDY; ESCHERICHIA COLI; HEAT SHOCK; IN VITRO STUDY; MOLECULAR SIZE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN FUNCTION;

BACTERIAL PROTEINS; CARBOXY-LYASES; DNA-DIRECTED RNA POLYMERASES; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HEAT-SHOCK RESPONSE; HOT TEMPERATURE; INCLUSION BODIES; KINETICS; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; MUTATION; PROMOTER REGIONS, GENETIC; PROTEIN DENATURATION; PROTEIN REFOLDING; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SIGMA FACTOR; URIDINE PHOSPHORYLASE;

ESCHERICHIA COLI;

EID: 84862812281     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.02.051     Document Type: Article

References (30)

1. J.N. Phue, and J. Shiloach Transcription levels of key metabolic genes are the cause for different glucose utilization pathways in E. coli B (BL21) and E. coli K (JM109) J. Biotechnol. 109 2004 21 30 (Pubitemid 38452568)
2. J.N. Phue, and J. Shiloach Impact of dissolved oxygen concentration on acetate accumulation and physiology of E. coli BL21, evaluating transcription levels of key genes at different dissolved oxygen conditions Metab. Eng. 7 2005 353 363 (Pubitemid 41790466)
3. F. Baneyx, and M. Mujacic Recombinant protein folding and misfolding in Escherichia coli Nat. Biotechnol. 22 2004 1399 1408
4. U. Jakob, W. Muse, M. Eser, and J.C. Bardwell Chaperone activity with a redox switch Cell 96 1999 341 352 (Pubitemid 29077588)
5. F.U. Hartl, and M. Hayer-Hartl Molecular chaperones in the cytosol: from nascent chain to folded protein Science 295 2002 1852 1858 (Pubitemid 34214115)
6. A. Mogk, T. Tomoyasu, P. Goloubinoff, S. Rüdiger, D. Röder, H. Langen, and B. Bukau Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB EMBO J. 18 1999 6934 6949 (Pubitemid 30000447)
7. R.S. Ullers, J. Luirink, N. Harms, F. Schwager, C. Georgopoulos, and P. Genevaux SecB is a bona fide generalized chaperone in Escherichia coli Proc. Natl. Acad. Sci. USA 101 2004 7583 7588 (Pubitemid 38658072)
8. W.J. Netzer, and F.U. Hartle Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms Trends Biochem. Sci. 23 1998 68 73 (Pubitemid 28085230)
9. G.H. Lorimer A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo FASEB J. 10 1996 5 9 (Pubitemid 26035500)
10. U. Rinas, F. Hoffmann, E. Betiku, D. Estapé, and S. Marten Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli J. Biotechnol. 127 2007 244 257 (Pubitemid 46107138)
11. T. Tomoyasu, A. Mogk, H. Langen, P. Goloubinoff, and B. Bukau Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol Mol. Microbiol. 40 2001 397 413 (Pubitemid 32391634)
12. K.Y. Han, J.S. Park, H.S. Seo, K.Y. Ahn, and J. Lee Multiple stressor-induced proteome responses of Escherichia coli BL21(DE3) J. Proteome. Res. 7 2008 1891 1903
13. M. Karberg, H. Guo, J. Zhong, R. Coon, J. Perutka, and A.M. Lambowitz Group II introns as controllable gene targeting vectors for genetic manipulation of bacteria Nat. Biotechnol. 19 2001 1162 1167 (Pubitemid 33115703)
14. B.I. Kurganov, A.A. Burlakova, V.Y. Chernyak, and V.G. Debabov Denaturation of uridine phosphorylase from Escherichia coli K-12 by guanidine hydrochloride Biochem. Mol. Biol. Int. 41 1997 1191 1199 (Pubitemid 27232078)
15. J.C. Leer, K. Hammer-Jespersen, and M. Schwartz Uridine phosphorylase from Escherichia coli. Physical and chemical characterization Eur. J. Biochem. 75 1977 217 224 (Pubitemid 8080831)
16. J. Winter, K. Linke, A. Jatzek, and U. Jakob Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33 Mol. Cell 17 2005 381 392 (Pubitemid 40193309)
17. I. Wagner, H. Arlt, L. van Dyck, T. Langer, and W. Neupert Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria EMBO J. 13 1994 5135 5145 (Pubitemid 24341095)
18. 32 in vivo J. Biol. Chem. 280 2005 17758 17768 (Pubitemid 41389014)
19. 32, reveals a multifaceted cellular response to heat stress Genes Dev. 20 2006 1776 1789 (Pubitemid 43992886)
20. B.K. Cho, K. Zengler, Y. Qiu, Y.S. Park, E.M. Knight, C.L. Barrett, Y. Gao, and B.Ø. Palsson The transcription unit architecture of the Escherichia coli genome Nat. Biotechnol. 11 2009 1043 1049
21. S. Jozefczuk, S. Klie, G. Catchpole, J. Szymanski, A. Cuadros-Inostroza, D. Steinhauser, J. Selbig, and L. Willmitzer Metabolomic and transcriptomic stress response of Escherichia coli Mol. Syst. Biol. 6 2010 364
22. H.J. Oh, X. Chen, and J.R. Subjeck Hsp110 protects heat-denatured proteins and confers cellular thermoresistance J. Biol. Chem. 272 1997 31636 31640 (Pubitemid 28013309)
23. H. Schröder, T. Langer, F.U. Hartl, and B. Bukau DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage EMBO J. 12 1993 4137 4144 (Pubitemid 23302027)
24. E. Basha, G.J. Lee, L.A. Breci, A.C. Hausrath, N.R. Buan, K.C. Giese, and E. Vierling The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions J. Biol. Chem. 279 2004 7566 7575 (Pubitemid 38294635)
25. K. Liberek, A. Lewandowska, and S. Zietkiewicz Chaperones in control of protein disaggregation EMBO J. 27 2008 328 335 (Pubitemid 351161659)
26. R.L. van Montfort, E. Basha, K.L. Friedrich, C. Slingsby, and E. Vierling Crystal structure and assembly of a eukaryotic small heat shock protein Nat. Struct. Biol. 8 2001 1025 1030 (Pubitemid 33101621)
27. M. Haslbeck, S. Walke, T. Stromer, M. Ehrnsperger, H.E. White, S. Chen, H.R. Saibil, and J. Buchner Hsp26: a temperature-regulated chaperone EMBO J. 18 1999 6744 6751
28. R. Shashidharamurthy, H.A. Koteiche, J. Dong, and H.S. McHaourab Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme J. Biol. Chem. 280 2005 5281 5289 (Pubitemid 40280001)
29. J.A. Song, D.S. Lee, J.S. Park, K.Y. Han, and J. Lee The N-domain of Escherichia coli phosphoglycerate kinase is a novel fusion partner to express aggregation-prone heterologous proteins Biotechnol. Bioeng. 109 2 2012 325 335
30. J.S. Park, K.Y. Han, J.H. Lee, J.A. Song, K.Y. Ahn, H.S. Seo, S.J. Sim, S.W. Kim, and J. Lee Solubility enhancement of aggregation-prone heterologous proteins by fusion expression using stress-responsive Escherichia coli protein, RpoS BMC Biotechnol. 8 2008 15