Expression and purification of the transmembrane domain of Fukutin-I for biophysical studies

Protein Expression and Purification

Volumn 72, Issue 1, 2010, Pages 107-112

  Marius, P ^a   Wright, J N ^a   Findlow, I S ^a   Williamson, P T F ^a  

^a UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

Author keywords

Expression; Purification; Solid state NMR; Transmembrane peptides

Indexed keywords

FCMD PROTEIN, MOUSE; PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; MOLECULAR GENETICS; MOUSE; NUCLEAR MAGNETIC RESONANCE; PLASMID; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; ESCHERICHIA COLI; GENE EXPRESSION; MASS SPECTROMETRY; MICE; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 77951135980     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.01.019     Document Type: Article

References (20)

1. Martin-Rendon E., and Blake D.J. Protein glycosylation in disease: new insights into the congenital muscular dystrophies. Trends Pharmacol. Sci. 24 (2003) 178-183
2. Torelli S., Brown S.C., Brockington M., Dolatshad N.F., Jimenez C., Skordis L., Feng L.H., Merlini L., Jones D.H., Romero N., Wewer U., Voit T., Sewry C.A., Noguchi S., Nishino I., and Muntoni F. Sub-cellular localisation of fukutin related protein in different cell lines and in the muscle patients with MDC1C and LGMD2I. Neuromuscul. Disord. 15 (2005) 836-843
3. Keramaris-Vrantsis E., Lu P.J., Doran T., Zillmer A., Ashar J., Esapa C.T., Benson M.A., Blake D.J., Rosenfeld J., and Lu Q.L. Fukutin-related protein localizes to the Golgi apparatus and mutations lead to mislocalization in muscle in vivo. Muscle Nerve 36 (2007) 455-465
4. Matsumoto H., Noguchi S., Sugie K., Ogawa M., Murayama K., Hayashi Y.K., and Nishino I. Subcellular localization of fukutin and fukutin-related protein in muscle cells. J. Biochem. 135 (2004) 709-712
5. Lommel M., Willer T., and Strahl S. POMT2, a key enzyme in Walker-Warburg syndrome: somatic sPOMT2, but not testis-specific tPOMT2, Is crucial for mannosyltransferase activity in vivo. Glycobiology 18 (2008) 615-625
6. Opat A.S., van Vliet C., and Gleeson P.A. Trafficking and localisation of resident Golgi glycosylation enzymes. Biochimie 83 (2001) 763-773
7. Munro S. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J. 14 (1995) 4695-4704
8. Munro S. Localization of proteins to the Golgi apparatus. Trends Cell Biol. 8 (1998) 11-15
9. Esapa C.T., Benson M.A., Schroder J.E., Martin-Rendon E., Brockington M., Brown S.C., Muntoni F., Kroger S., and Blake D.J. Functional requirements for fukutin-related protein in the Golgi apparatus. Hum. Mol. Genet. 11 (2002) 3319-3331
10. Pelham H.R.B., and Munro S. Sorting of membrane proteins in the secretory pathway. Cell 75 (1993) 603-605
11. Rayner J.C., and Pelham H.R.B. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16 (1997) 1832-1841
12. Hong M., and Jakes K. Selective and extensive C-13 labeling of a membrane protein for solid-state NMR investigations. J. Biomol. NMR 14 (1999) 71-74
13. Higman V.A., Flinders J., Hiller M., Jehle S., Markovic S., Fiedler S., van Rossum B.J., and Oschkinat H. Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins. J. Biomol. NMR 44 (2009) 245-260
14. Hu J., Qin H., Li C., Sharma M., Cross T.A., and Gao F.P. Structural biology of transmembrane domains: efficient production and characterization of transmembrane peptides by NMR. Protein Sci. 16 (2007) 2153-2165
15. Sambrook J., and Russell D.W. Molecular Cloning: A Laboratory Manual (2001), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
16. Schagger H., and Vonjagow G. Tricine sodium dodecyl-sulfate-polyacrylamide-gel electrophoresis for the separation of proteins in the range from 1-Kda to 100-Kda. Anal. Biochem. 166 (1987) 368-379
17. Whitmore L., and Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89 (2008) 392-400
18. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
19. Gasteiger E., Gattiker A., Hoogland C., Ivanyi I., Appel R.D., and Bairoch A. ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 31 (2003) 3784-3788
20. Cavanagh J., Fairbrother W.J., Palmer A.G., and Skelton N.J. Protein NMR Spectroscopy: Principles and Practice (2007), Elsevier Academic Press, San Diego, CA