Selection and Structure of Hyperactive Inteins: Peripheral Changes Relayed to the Catalytic Center

Journal of Molecular Biology

Volumn 393, Issue 5, 2009, Pages 1106-1117

  Hiraga, Kaori ^a   Soga, Ikko ^a,b   Dansereau, John T ^a   Pereira, Brian ^a,c   Derbyshire, Victoria ^a   Du, Zhenming ^d   Wang, Chunyu ^d   Van Roey, Patrick ^a   Belfort, Georges ^c   Belfort, Marlene ^a,b  

^a WADSWORTH CENTER   (United States)

^b STATE UNIVERSITY OF NEW YORK   (United States)

^c RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^d Research Rensselaer Polytechnic Institute   (United States)

Author keywords

intein application; intramolecular intein communication; robust intein mutants

Indexed keywords

INTEIN;

ALLOSTERISM; ARTICLE; BIOTECHNOLOGY; CATALYSIS; CONTROLLED STUDY; ESCHERICHIA COLI; GENE MUTATION; IN VITRO STUDY; NONHUMAN; PEPTIDE MAPPING; PH; PHAGE DISPLAY; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN ISOLATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; TEMPERATURE;

AMINO ACID SEQUENCE; BIOCATALYSIS; CHITIN; CRYSTALLOGRAPHY, X-RAY; INTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; MYCOBACTERIUM TUBERCULOSIS; PEPTIDE LIBRARY; PHENOTYPE; PROTEIN SPLICING; PROTEIN STRUCTURE, SECONDARY; RESINS, SYNTHETIC;

EID: 70350008258     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.074     Document Type: Article

References (38)

1. Paulus H. Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69 (2000) 447-496
2. Wood D., Wu W., Belfort G., Derbyshire V., and Belfort M. A genetic system yields self-cleaving inteins for bioseparations. Nat. Biotechnol. 17 (1999) 889-892
3. Perler F.B., and Adam E. Protein splicing and its applications. Curr. Opin. Biotechnol. 11 (2000) 377-383
4. Buskirk A.R., Ong Y.C., Gartner Z.J., and Liu D.R. Directed evolution of ligand dependence: small-molecule-activated protein splicing. Proc. Natl Acad. Sci. USA 101 (2004) 10505-10510
5. Muralidharan V., and Muir T.W. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat. Methods 3 (2006) 429-438
6. 18F-labeling of the protein hormone leptin using a general two-step ligation procedure. J. Am. Chem. Soc. 130 (2008) 9106-9112
7. Amitai G., Callahan B.P., Stanger M.J., Belfort G., and Belfort M. Modulation of intein activity by its neighboring extein substrates. Proc. Natl Acad. Sci. USA 106 (2009) 11005-11010
8. Lockless S.W., and Muir T.W. Traceless protein ligation utilizing evolved split inteins. Proc. Natl Acad. Sci. USA 106 (2009) 10999-11004
9. Noren C.J., Wang J., and Perler F.B. Dissecting the chemistry of protein splicing and its applications. Angew. Chem., Int. Ed. Engl. 39 (2000) 450-466
10. Wu W., Wood D.W., Belfort G., Derbyshire V., and Belfort M. Intein-mediated purification of cytotoxic endonuclease I-TevI by insertional inactivation and pH-controllable splicing. Nucleic Acids Res. 30 (2002) 4864-4871
11. Evans T.C., and Xu M.Q. Mechanistic and kinetic considerations of protein splicing. Chem. Rev. 102 (2002) 4869-4884
12. Chong S., Mersha F.B., Comb D.G., Scott M.E., Landry D., Vence L.M., et al. Single-column purification of free recombinant proteins using a self-cleavage affinity tag derived from a protein splicing element. Gene 192 (1997) 271-281
13. Chong S., Montello G.E., Zhang A., Cantor E.J., Liao W., Xu M.Q., and Benner J. Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step. Nucleic Acids Res. 26 (1998) 5109-5115
14. Wood D.W., Derbyshire V., Wu W., Chartrain M., Belfort M., and Belfort G. Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor. Biotechnol. Prog. 16 (2000) 1055-1063
15. Paulus H. Protein splicing inhibitors as a new class of antimycobacterial agents. Drugs Future 32 (2007) 973-984
16. Adam E., and Perler F.B. Development of a positive genetic selection system for inhibition of protein splicing using mycobacterial inteins in Escherichia coli DNA gyrase subunit A. J. Mol. Microbiol. Biotechnol. 4 (2002) 479-487
17. Cann I.K., Amaya K.R., Southworth M.W., and Perler F.B. Bacteriophage-based genetic system for selection of nonsplicing inteins. Appl. Environ. Microbiol. 70 (2004) 3158-3162
18. Zeidler M.P., Tan C., Bellaiche Y., Cherry S., Hader S., Gayko U., and Perrimon N. Temperature-sensitive control of protein activity by conditionally splicing inteins. Nat. Biotechnol. 22 (2004) 871-876
19. Skretas G., and Wood D.W. Regulation of protein activity with small-molecule-controlled inteins. Protein Sci. 14 (2005) 523-532
20. Derbyshire V., Wood D.W., Wu W., Dansereau J.T., Dalgaard J.Z., and Belfort M. Genetic definition of a protein-splicing domain: functional mini-inteins support structure predictions and a model for intein evolution. Proc. Natl Acad. Sci. USA 94 (1997) 11466-11471
21. Hiraga K., Derbyshire V., Dansereau J.T., Van Roey P., and Belfort M. Minimization and stabilization of the Mycobacterium tuberculosis recA intein. J. Mol. Biol. 354 (2005) 916-926
22. Hashimoto M., Ikegami T., Seino S., Ohuchi N., Fukada H., Sugiyama J., et al. Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12. J. Bacteriol. 182 (2000) 3045-3054
23. Wang J.Y., and Chao Y.P. Immobilization of cells with surface-displayed chitin-binding domain. Appl. Environ. Microbiol. 72 (2006) 927-931
24. Van Roey P., Pereira B., Li Z., Hiraga K., Belfort M., and Derbyshire V. Crystallographic and mutation studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue. J. Mol. Biol. 367 (2007) 162-173
25. Mills K.V., and Paulus H. Reversible inhibition of protein splicing by zinc ion. J. Biol. Chem. 276 (2001) 10832-10838
26. Gangopadhyay J.P., Jiang S.-Q., van Berkel P., and Paulus H. In vitro splicing of erythropoietin by the Mycobacterium tuberculosis RecA intein without substituting amino acids at the splice junctions. Biochim. Biophys. Acta 1619 (2003) 193-200
27. Gangopadhyay J.P., Jiang S.Q., and Paulus H. An in vitro screening system for protein splicing inhibitors based on green fluorescent protein as an indicator. Anal. Chem. 75 (2003) 2456-2462
28. Crameri A., Whitehorn E.A., Tate E., and Stemmer W.P. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14 (1996) 315-319
29. Pietrokovski S. Modular organization of inteins and C-terminal autocatalytic domains. Protein Sci. 7 (1998) 64-71
30. Pietrokovski S. Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins. Protein Sci. 3 (1994) 2340-2350
31. Perler F.B., Olsen G.J., and Adam E. Compilation and analysis of intein sequences. Nucleic Acids Res. 25 (1997) 1087-1093
32. Pearl E.J., Tyndall J.D., Poulter R.T., and Wilbanks S.M. Sequence requirements for splicing by the Cne PRP8 intein. FEBS Lett. 581 (2007) 3000-3004
33. Kumar S., and Nussinov R. Close-range electrostatic interactions in proteins. ChemBioChem 3 (2002) 604-617
34. Sibille N., Favier A., Azuaga A.I., Ganshaw G., Bott R., Bonvin A.M., et al. Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase. Protein Sci. 15 (2006) 1915-1927
35. Slonczewski J.L., Rosen B.P., Alger J.R., and Macnab R.M. pH homeostasis in Escherichia coli: measurement by 31P nuclear magnetic resonance of methylphosphonate and phosphate. Proc. Natl Acad. Sci. USA 78 (1981) 6271-6275
36. Baruah G.L., Couto D., and Belfort G. A predictive aggregate transport model for microfiltration of combined macromolecular solutions and poly-disperse suspensions: testing model with transgenic goat milk. Biotechnol. Prog. 19 (2003) 1533-1540
37. Hunter C.V., Tiley L.S., and Sang H.M. Developments in transgenic technology: applications for medicine. Trends Mol. Med. 11 (2005) 293-298
38. Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., and Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77 (1989) 61-68