Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: A possibility of protein stabilization tag

PLoS ONE

Volumn 6, Issue 1, 2011, Pages

  Takano, Kazufumi ^a,b   Okamoto, Tomohiro ^a   Okada, Jun ^a   Tanaka, Shun Ichi ^a   Angkawidjaja, Clement ^a   Koga, Yuichi ^a   Kanaya, Shigenori ^a  

^a OSAKA UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; RIBONUCLEASE; SULFOLOBUS TOKODAII CARBOXY TERMINAL RIBONUCLEASE HI; UNCLASSIFIED DRUG; HYBRID PROTEIN; RIBONUCLEASE H; RIBONUCLEASE HI;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; HYPERTHERMOPHILE; NONHUMAN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN STABILITY; RESIDUE ANALYSIS; SULFOLOBUS TOKODAII; THERMODYNAMICS; WILD TYPE; AMINO ACID SEQUENCE; CHEMISTRY; ENZYMOLOGY; GENETIC VARIABILITY; GENETICS; SULFOLOBUS; TECHNIQUE;

SULFOLOBUS TOKODAII;

AMINO ACID SEQUENCE; GENETIC VARIATION; METHODS; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; RIBONUCLEASE H; SULFOLOBUS; THERMODYNAMICS;

EID: 79251638276     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0016226     Document Type: Article

References (33)

1. Trevino SR, Scholtz JM, Pace CN (2009) Increasing protein conformational stability by optimizing beta-turn sequence. J Mol Biol 373: 211-218.
2. Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, et al. (2009) Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Proc Natl Acad Sci USA 106: 2601-2606.
3. Kimura S, Nakamura H, Hashimoto T, Oobatake M, Kanaya S (1992) Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. J Biol Chem 267: 21535-21542.
4. Watanabe K, Ohkuri T, Yokobori S, Yamagishi A (2006) Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. J Mol Biol 355: 664-674.
5. Miyazaki K, Wintrode PL, Grayling RA, Rubingh DN, Arnold FH (2000) Directed evolution study of temperature adaptation in a psychrophilic enzyme. J Mol Biol 297: 1015-1026.
6. Tadokoro T, Matsushita K, Abe Y, Rohman MS, Koga Y, et al. (2008) Remarkable stabilization of a psychrotrophic RNase HI by a combination of thermostabilizing mutations identified by the suppressor mutation method. Biochemistry 47: 8040-8047.
7. Porath J, Carlsson J, Olsson I, Belfrage G (1975) Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258: 598-599.
8. Hopp TP (1988) A short polypeptide marker sequence useful for recombinant protein identification and purification. Bio/Technology 6: 1204-1210.
9. Kato A, Maki K, Ebina T, Kuwajima K, Soda K, et al. (2007) Mutational analysis of protein solubility enhancement using short peptide tags. Biopolymers 85: 12-18.
10. Kondo N, Ebihara A, Ru H, Kuramitsu S, Iwamoto A, et al. (2009) Thermus thermophilus-derived protein tags that aid in preparation of insoluble viral proteins. Anal Biochem 385: 278-285.
11. Söling A, Simm A, Rainov N (2002) Intracellular localization of Herpes simplex virus type 1 thymidine kinase fused to different fluorescent proteins depends on choice of fluorescent tag. FEBS Lett 527: 153-158.
12. Hailey DW, Davis TN, Muller EGD (2002) Fluorescence resonance energy transfer using colour variants of green fluorescent protein. Methods Enzymol 351: 34-49.
13. You DJ, Chon H, Koga Y, Takano K, Kanaya S (2006) Crystallization and preliminary crystallographic analysis of type 1 RNase H from the hyperthermophilic archaeon Sulfolobus tokodaii 7. Acta Crystallogr F62: 781-784.
14. You DJ, Chon H, Koga Y, Takano K, Kanaya S (2007) Crystal structure of type 1 ribonuclease H from hyperthermophilic archaeon Sulfolobus tokodaii: role of arginine 118 and C-terminal anchoring. Biochemistry 46: 11494-11503.
15. Okada J, Okamoto T, Mukaiyama A, Tadokoro T, You DJ, et al. (2010) Evolution and thermodynamics of slow unfolding of hyperstable monomeric proteins. BMC Evol Biol 10: 207.
16. Tadokoro T, You DJ, Abe Y, Chon H, Matsumura H, et al. (2007) Structural, thermodynamic, and mutational analyses of a psychrotrophic RNase HI. Biochemistry 46: 7460-7468.
17. Kanaya S, Katsuda C, Kimura S, Nakai T, Kitakuni E, et al. (1991) Stabilization of Escherichia coli ribonuclease H by introduction of an artificial disulfide bond. J Biol Chem 266: 6038-6044.
18. Otwinowski Z, Minor W (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
19. Vagin A, Teplyakov A (1997) MOLREP: an automated program for molecular replacement export. J Appl Crystallogr 30: 1022-1025.
20. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr A47: 110-119.
21. Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D60: 2126-2132.
22. Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D53: 240-255.
23. Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK - a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283-291.
24. Razvi A, Scholtz JM (2006) Lessons in stability from thermophilic proteins. Protein Sci 15: 1569-1578.
25. Mukaiyama A, Takano K, Haruki M, Morikawa M, Kanaya S (2004) Kinetically robust monomeric protein from a hyperthermophile. Biochemistry 43: 13859-13866.
26. Dong H, Mukaiyama A, Tadokoro T, Koga Y, Takano K, et al. (2008) Hydrophobic effect on the stability and folding of a hyperthermophilic protein. J Mol Biol 378: 264-272.
27. Matsuura T, Miyai K, Trakulnaleamsai S, Yomo T, Shima Y, et al. (1999) Evolutionary molecular engineering by random elongation mutagenesis. Nat Biotechnol 17: 58-61.
28. Haruki M, Noguchi E, Akasako A, Oobatake M, Itaya M, et al. (1994) A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. J Biol Chem 269: 26904-26911.
29. Fu Y, Luo Y (2010) The N-terminal integrity is critical for the stability and biological functions of endostatin. Biochemistry 49: 6420-6429.
30. Takano K, Endo S, Mukaiyama A, Chon H, Matsumura H, et al. (2006) Structure of amyloid beta fragments in aqueous environments. FEBS J 273: 150-158.
31. Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, et al. (2006) Conformational contagion in a protein: structural properties of a chameleon sequence. Proteins 68: 617-625.
32. Wang M, Feng Y, Yao H, Wang J (2010) Importance of the C-terminal loop L137-S141 for the folding and folding stability of staphylococcal nuclease. Biochemistry 49: 4318-4326.
33. Schulenburg C, Weininger U, Neumann P, Meiselbach H, Stubbs MT, et al. (2010) Impact of the C-terminal disulfide bond on the folding and stability of onconase. Chembiochem 11: 978-986.