Engineering human MEK-1 for structural studies: A case study of combinatorial domain hunting

Journal of Structural Biology

Volumn 177, Issue 2, 2012, Pages 329-334

  Meier, Christoph ^a   Brookings, Daniel C ^a   Ceska, Thomas A ^a   Doyle, Carl ^a   Gong, Haiping ^a   McMillan, David ^a   Saville, Giles P ^a   Mushtaq, Adeel ^b   Knight, David ^b   Reich, Stefanie ^b   Pearl, Laurence H ^b,c   Powell, Keith A ^b   Savva, Renos ^b,d   Allen, Rodger A ^a  

^a UCB PHARMA   (Belgium)

^b Domainex Ltd   (United Kingdom)

^c UNIVERSITY OF SUSSEX   (United Kingdom)

^d UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

Domain hunting; Gene fragmentation; MEK 1; Protein expression; Structural biology

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE KINASE 1;

ANALYTIC METHOD; ARTICLE; COMBINATORIAL DOMAIN HUNTING; CRYSTAL STRUCTURE; CRYSTALLIZATION; HUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN TARGETING;

CLONING, MOLECULAR; CRYSTALLIZATION; CRYSTALLOGRAPHY; ESCHERICHIA COLI; HUMANS; MAP KINASE KINASE 1; PEPTIDE FRAGMENTS; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 84857030102     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.01.002     Document Type: Article

References (34)

1. An Y., Meresse P., Mas P.J., Hart D.J. CoESPRIT: a library-based construct screening method for identification and expression of soluble protein complexes. PLoS ONE 2011, 6:e16261.
2. Au K., Berrow N.S., Blagova E., Boucher I.W., Boyle M.P., et al. Application of high-throughput technologies to a structural proteomics-type analysis of Bacillus anthracis. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:1267-1275.
3. Barretto N., Jukneliene D., Ratia K., Chen Z., Mesecar A.D., et al. The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity. J. Virol. 2005, 79:15189-15198.
4. Cohen S.L., Chait B.T. Mass spectrometry as a tool for protein crystallography. Annu. Rev. Biophys. Biomol. Struct. 2001, 30:67-85.
5. Cornvik T., Dahlroth S.L., Magnusdottir A., Herman M.D., Knaust R., et al. Colony filtration blot: a new screening method for soluble protein expression in Escherichia coli. Nat. Methods 2005, 2:507-509.
6. Cowley S., Paterson H., Kemp P., Marshall C.J. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells. Cell 1994, 77:841-852.
7. DeLano W.L. The PyMOL Molecular Graphics System 2002, Schrödinger, LLC., Portland, OR.
8. Dyson M.R., Perera R.L., Shadbolt S.P., Biderman L., Bromek K., et al. Identification of soluble protein fragments by gene fragmentation and genetic selection. Nucleic Acids Res. 2008, 36:e51.
9. Edwards A.M., Arrowsmith C.H., Christendat D., Dharamsi A., Friesen J.D., et al. Protein production: feeding the crystallographers and NMR spectroscopists. Nat. Struct. Biol. 2000, 7(Suppl.):970-972.
10. English J.M., Cobb M.H. Pharmacological inhibitors of MAPK pathways. Trends Pharmacol. Sci. 2002, 23:40-45.
11. Fang J.Y., Richardson B.C. The MAPK signalling pathways and colorectal cancer. Lancet Oncol. 2005, 6:322-327.
12. Gao X., Bain K., Bonanno J.B., Buchanan M., Henderson D., et al. High-throughput limited proteolysis/mass spectrometry for protein domain elucidation. J. Struct. Func. Genom. 2005, 6:129-134.
13. Humphreys D.P., Bowering L. Production of Antibody Fab' Fragments in E. coli, p. xv, 889 p., 816 p. of plates. Therapeutic Monoclonal Antibodies: From Bench to Clinic 2009, John Wiley & Sons, Hoboken, NJ. Z. An (Ed.).
14. Kosako H., Gotoh Y., Nishida E. Requirement for the MAP kinase kinase/MAP kinase cascade in Xenopus oocyte maturation. EMBO J. 1994, 13:2131-2138.
15. Laing V.E., Brookings D.C., Carbery R.J., Simorte J.G., Hutchings M.C., et al. Fused thiophene derivatives as MEK inhibitors. Bioorg. Med. Chem. Lett. 2012, 22:472-475.
16. Lemieux E., Bergeron S., Durand V., Asselin C., Saucier C., et al. Constitutively active MEK1 is sufficient to induce epithelial-to-mesenchymal transition in intestinal epithelial cells and to promote tumor invasion and metastasis. Int. J. Cancer 2009, 125:1575-1586.
17. Linding R., Jensen L.J., Diella F., Bork P., Gibson T.J., et al. Protein disorder prediction: implications for structural proteomics. Structure 2003, 11:1453-1459.
18. Littler E. Combinatorial Domain Hunting: solving problems in protein expression. Drug Discov. Today 2010.
19. Maclagan K., Tommasi R., Laurine E., Prodromou C., Driscoll P.C., et al. A combinatorial method to enable detailed investigation of protein-protein interactions. Future Med. Chem. 2011, 3:271-282.
20. Mooij W.T., Mitsiki E., Perrakis A. ProteinCCD: enabling the design of protein truncation constructs for expression and crystallization experiments. Nucleic Acids Res. 2009, 37:W402-405.
21. Ohren J.F., Chen H., Pavlovsky A., Whitehead C., Zhang E., et al. Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat. Struct. Mol. Biol. 2004, 11:1192-1197.
22. Pages G., Lenormand P., L'Allemain G., Chambard J.C., Meloche S., et al. Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation. Proc. Natl. Acad. Sci. U S A 1993, 90:8319-8323.
23. Pearson G., English J.M., White M.A., Cobb M.H. ERK5 and ERK2 cooperate to regulate NF-kappaB and cell transformation. J. Biol. Chem. 2001, 276:7927-7931.
24. Pedelacq J.-D., Cabantous S., Terwilliger T.C., Waldo G.S. Split-GFP as a tool for finding soluble protein domains. Acta Crystallogr. A 2007, 63:s12-s13.
25. Pedelacq J.D., Nguyen H.B., Cabantous S., Mark B.L., Listwan P., et al. Experimental mapping of soluble protein domains using a hierarchical approach. Nucleic Acids Res 2011.
26. Reich S., Puckey L.H., Cheetham C.L., Harris R., Ali A.A., et al. Combinatorial Domain Hunting: An effective approach for the identification of soluble protein domains adaptable to high-throughput applications. Protein Sci. 2006, 15:2356-2365.
27. Robbins D.J., Zhen E., Owaki H., Vanderbilt C.A., Ebert D., et al. Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro. J. Biol. Chem. 1993, 268:5097-5106.
28. Santen R.J., Song R.X., McPherson R., Kumar R., Adam L., et al. The role of mitogen-activated protein (MAP) kinase in breast cancer. J. Steroid Biochem. Mol. Biol. 2002, 80:239-256.
29. Skarzynski T., Thorpe J. Industrial perspective on X-ray data collection and analysis. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:102-107.
30. Tarendeau F., Boudet J., Guilligay D., Mas P.J., Bougault C.M., et al. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat. Struct. Mol. Biol. 2007, 14:229-233.
31. Voisin L., Julien C., Duhamel S., Gopalbhai K., Claveau I., et al. Activation of MEK1 or MEK2 isoform is sufficient to fully transform intestinal epithelial cells and induce the formation of metastatic tumors. BMC Cancer 2008, 8:337.
32. Wu X., Noh S.J., Zhou G., Dixon J.E., Guan K.L. Selective activation of MEK1 but not MEK2 by A-Raf from epidermal growth factor-stimulated Hela cells. J. Biol. Chem. 1996, 271:3265-3271.
33. Yumerefendi H., Tarendeau F., Mas P.J., Hart D.J. ESPRIT: An automated, library-based method for mapping and soluble expression of protein domains from challenging targets. J. Struct. Biol. 2010, 271.
34. Zheng C.F., Guan K.L. Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2. J. Biol. Chem. 1993, 268:11435-11439.