Structure analysis of the membrane protein TatCd from the Tat system of B. subtilis by circular dichroism

Biochimica et Biophysica Acta - Biomembranes

Volumn 1788, Issue 10, 2009, Pages 2238-2244

  Nolandt, Olga V ^a   Walther, Torsten H ^b   Roth, Siegmar ^a   Bürck, Jochen ^a   Ulrich, Anne S ^a,b  

^a KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

^b UNIVERSITY OF KARLSRUHE   (Germany)

Author keywords

Circular dichroism (CD); Oriented circular dichroism (OCD); TatCd; Twin arginine translocation (Tat) Membrane protein

Indexed keywords

MEMBRANE PROTEIN; TATCD PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; ARTIFICIAL MEMBRANE; BACILLUS SUBTILIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ESCHERICHIA COLI; LIPID BILAYER; MEMBRANE BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ARGININE; BACILLUS SUBTILIS; CIRCULAR DICHROISM; CLONING, MOLECULAR; ESCHERICHIA COLI; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 70349481163     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.07.003     Document Type: Article

References (35)

1. Sargent F., Bogsch E., Stanley M., Wexler M., Robinson C., Berks B., and Palmer T. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17 (1998) 3640-3650
2. Robinson C., and Bolhuis A. Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim. Biophys. Acta 1694 (2004) 135-147
3. Berks B., Palmer T., and Sargent F. Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. Curr. Opin. Microbiol. 8 (2005) 174-181
4. Sargent F. The twin-arginine transport system: Moving folded proteins across membranes. Biochem. Soc. Trans. 35 (2007) 835-847
5. Punginelli C., Maldonado B., Grahl S., Jack R., Alami M., Schröder J., Berks B.C., and Palmer T. Cysteine scanning mutagenesis and topological mapping of the Escherichia coli twin-arginine translocase TatC component. J. Bacteriol. 189 (2007) 5482-5494
6. http://www.uniprot.org/uniprot/P42252
7. Jongbloed J.D., Grieger U., Antelmann H., Hecker M., Nijland R., Bron S., and van Dijl J.M. Two minimal Tat translocases in Bacillus. Mol. Microbiol. 54 (2004) 1319-1325
8. Jongbloed J.D., Martin U., Antelmann H., Hecker M., Tjalsma H., Venema G., Bron S., van Dijl J.M., and Muller J. TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway. J. Biol.Chem. 275 (2000) 41350-41357
9. Sturm A., Schierhorn A., Lindenstrauss U., Lilie H., and Bruser T. YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins. J. Biol. Chem. 281 (2006) 13972-13978
10. Barnett J.P., Eijlander R.T., Kuipers O.P., and Robinson C. A minimal Tat system from a gram-positive organism: A bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J. Biol. Chem. 283 (2008) 2534-2542
11. Schreiber S., Stengel R., Westermann M., Volkmer-Engert R., Pop O.I., and Müller J.P. Affinity of TatCd for TatAd elucidates its receptor function in the Bacillus subtilis twin arginine translocation (Tat) translocase system. J. Biol. Chem. 281 (2006) 19977-19984
12. Lange C., Muller S.D., Walther T.H., Bürck J., and Ulrich A.S. Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach. Biochim. Biophys. Acta 1768 (2007) 2627-2634
13. 15N-NMR. Biochim. Biophys. Acta 1768 (2007) 3071-3079
14. Kelly S.M., Jess T.J., and Price N.C. How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751 (2005) 119-139
15. Berova N., Nakanishi K., and Woody R.W. Circular Dichroism: Principles and Applications. second ed. (2000), Wiley-VCH, Weinheim
16. Cabos-Siguier B., Steunou A.L., Joseph G., Alazard R.T., Ducoux-Petit M., Nieto L., Monsarrat B., Erard M., and Clotte E. Expression and purification of human full-length N Oct-3, a transcription factor involved in melanoma growth. Protein Expr. Purif. 64 (2009) 39-46
17. Gustafsson E., Forsberg C., Haraldsson K., Lindman S., Ljung L., and Furebring C. Purification of truncated and mutated chemotaxis inhibitory protein of Staphylococcus aureus-an anti-inflammatory protein. Protein Expr. Purif. 63 (2009) 95-101
18. Cyr N., Madrid K.P., Strasser R., Aurousseau M., Finn R., Ausio J., and Jardi A. Leishmania donovani peroxin 14 undergoes a marked conformational change following association with peroxin 5. J. Biol. Chem. 283 (2008) 31488-31499
19. Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
20. Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6 (1967) 1948-1954
21. Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
22. Provencher S.W., and Glockner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20 (1981) 33-37
23. van Stokkum I.H.M., Spoelder H.J.W., Bloemendal M., van Grondelle R., and Groen F.C.A. Estimation of protein secondary structure and error analysis from CD spectra. Anal. Biochem. 191 (1990) 110-118
24. Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
25. Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) W668-673
26. Lobley A., Whitmore L., and Wallace B.A. DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18 (2002) 211-212
27. Bürck J., Roth S., Wadhwani P., Afonin S., Strandberg E., and Ulrich A.S. Conformation and membrane orientation of amphiphilic helical peptides by oriented circular dichroism. Biophys. J. 95 (2008) 3872-3881
28. Chen F.Y., Lee M.T., and Huang H.W. Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin. Biophys. J. 82 (2002) 908-914
29. Olah G.A., and Huang H.W. Circular dichroism of oriented α-helices: I. Proof of the exciton theory. J. Chem. Phys. 89 (1988) 2531-2538
30. Wu Y., Huang H.W., and Olah G.A. Method of oriented circular dichroism. Biophys. J. 57 (1990) 797-806
31. Vogel H. Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes. Biochemistry 26 (1987) 4562-4572
32. Wallace B.A., and Mao D. Circular dichroism analyses of membrane proteins: An examination of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets. Analytical Biochemistry 142 (1984) 317-328
33. II-type helical conformation for bacteriorhodopsin in the purple membrane. Biochemistry 28 (1989) 2134-2139
34. Solid State NMR Spectroscopy. Principles and Applications (2002), Blackwell Science Ltd., Oxford
35. 31P nuclear magnetic resonance and the group structure of phospholipids in membranes. Biochim. Biophys. Acta 512 (1978) 105-140