Mass spectrometric mapping of ion channel proteins (porins) and identification of their supramolecular membrane assembly

Proteins: Structure, Function and Genetics

Volumn 33, Issue SUPPL. 2, 1998, Pages 63-73

  Bühler, Stefan ^a   Michels, Jenny ^a   Wendt, Silke ^a,b   Rück, Alexander ^a   Brdiczka, Dieter ^a   Welte, Wolfram ^a   Przybylski, Michael ^a  

^a UNIVERSITY OF KONSTANZ   (Germany)

^b ETH ZURICH   (Switzerland)

Author keywords

In situ gel digestion; MALDI mass spectrometric peptide mapping; Membrane proteins; Noncovalent complexes; Permeability transition; Porin; Protein interactions

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; ION CHANNEL; MEMBRANE PROTEIN; PORIN; TRYPSIN; PEPTIDE;

AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; MASS SPECTROMETRY; MITOCHONDRIAL MEMBRANE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN PROTEIN INTERACTION; RHODOBACTER CAPSULATUS; CHEMISTRY; INTRACELLULAR MEMBRANE; METABOLISM; METHODOLOGY; MITOCHONDRION; PEPTIDE MAPPING; PROTEIN CONFORMATION;

BACTERIA (MICROORGANISMS); RHODOBACTER CAPSULATUS; RHODOPSEUDOMONAS;

ELECTROPHORESIS, POLYACRYLAMIDE GEL; INTRACELLULAR MEMBRANES; MITOCHONDRIA; PEPTIDE MAPPING; PEPTIDES; PORINS; PROTEIN CONFORMATION; RHODOBACTER CAPSULATUS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 0032252072     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(1998)33:2+<63::AID-PROT8>3.0.CO;2-I     Document Type: Article

References (39)

1. Arnott D., O'Connell K.L., King K.L., Stults J.T. An integrated approach to proteome analysis: identification of proteins associated with cardiac hypertrophy. Anal. Biochem. 258:1-18, 1998.
2. Przybylski M., Schnaible V., Kast J., et al. Approaches to the characterisation of tertiary and supramolecular protein structures by combination of protein chemistry and mass spectrometry. In: Ens W., editor. "New Methods for the Study of Biomolecular Complexes - A NATO Advanced Studies Series." Ens, W. (ed.). The Netherlands: Kluwer Academic Publishers, 1998:17-43.
3. Przybylski M., Kast J., Glocker M.O., et al. Mass spectrometric approaches to molecular characterization of protein-nucleic acid interactions. Toxicol. Lett. 82:567-575, 1995.
4. Suckau D., Kohl J., Karwath G., et al. Molecular epitope identification by limited proteolysis of an immobilised antigen-antibody complex and mass spectrometric peptide mapping. Proc. Natl. Acad. Sci. USA 87:9848-9852, 1990.
5. Svoboda M., Przybylski M., Schreurs J., Miyajima A., Hogeland K., Deinzer M. Mass spectrometric determination of glycosylation sites and oligosaccharide composition of insect-expressed mouse interleukin-3. J. Chromatogr. 562:403-419, 1991.
6. Krell T., Horsburgh M.J., Cooper A., Kelly S.M., Coggins J.R. Localization of the active site of type II dehydroquinases. Identification of a common arginine-containing motif in the two classes of dehydroquinases. J. Biol. Chem. 271:24492-24497, 1996.
7. Glocker M.O., Borchers C., Fiedler W., Suckau D., Przybylski M. Molecular characterization of surface topology in protein tertiary structures by amino-acylation and mass spectrometric peptide mapping. Biocon. Chem. 5:583-590, 1994.
8. Przybylski M., Glocker M.O., Nestel U., et al. X-ray crystallographic and mass spectrometric structure determination and functional characterization of succinylated porin from Rhodobacter capsulatus: implications for ion selectivity and single-channel conductance. Protein Sci. 5:1477-1489, 1996.
9. Suckau D., Mak M., Przybylski M. Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping. Proc. Natl. Acad. Sci. USA 89:5630-5634, 1992.
10. Mortz E., Vorm O., Mann M., Roepstorff P. Identification of proteins in polyacrylamide gels by mass spectrometric peptide mapping combined with database search. Biol. Mass Spectrom. 23:249-261, 1994.
11. Shevchenko A., Jensen O.N., Podtelejnikov A.V., et al. Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels. Proc. Natl. Acad. Sci. USA 93:14440-14445, 1996.
12. Kussmann M., Lassing U., Stürmer C.A., Przybylski M., Roepstorff P. Matrix-assisted laser desorption/ionization mass spectrometric peptide mapping of the neural cell adhesion protein neurolin purified by sodium dodecyl sulfate polyacrylamide gel electrophoresis or acidic precipitation. J. Mass Spectrom. 32:483-493, 1997.
13. Jensen O.N., Podtelejnikov A., Mann M. Delayed extraction improves specificity in database searches by matrix-assisted laser desorption/ionization peptide maps. Rapid Commun. Mass Spectrom. 10:1371-1378, 1996.
14. Jensen O.N., Podtelejnikov A.V., Mann M. Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. Anal. Chem. 69:4741-4750, 1997.
15. Schnaible V., Michels J., Zeth K., et al. Approaches to the characterisation of membrane channel proteins (porins) by UV MALDI-MS. Int. J. Mass Spec. Ion Proc. 169/170:165-177, 1997.
16. Welte W., Nestel U., Wacker T., Diederichs K. Structure and function of the porin channel. Kidney Int. 48:930-940, 1995.
17. Benz R. Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins. Biochim. Biophys. Acta 1197:167-196, 1994.
18. Nestel U., Wacker T., Woitzik D., Weckesser J., Kreutz W., Welte W. Crystallization and preliminary X-ray analysis of porin from Rhodobacter capsulatus. FEBS Lett. 242:405-408, 1989.
19. Colombini M. A candidate for the permeability pathway of the outer initochondrial membrane. Nature 279:643-645, 1979.
20. McEnery M.W. The mitochondrial benzodiazepine receptor: evidence for association with the voltage-dependent anion channel (VDAC). J. Biomembr. Bioenerg. 24:63-69, 1992.
21. Beutner G., Rück A., Riede B., Welte W., Brdiczka D. Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett. 396:189-195, 1996.
22. Zamzami N., Susin S.A., Marchetti P., et al. Mitochondrial control of nuclear apoptosis. J. Exp. Med. 183:1533-1544, 1996.
23. Susin S.A., Zamzami N., Castedo M., et al. Bcl-2 inhibits the mitochondrial release of an apoptogenic protease. J. Exp. Med. 184:1331-1341, 1996.
24. Pinto V., Benz R., Palmeri F. Interaction of non-classical detergents with the mitochondrial porin. Eur. J. Biochem. 183:179-187, 1989.
25. Bureau M.H., Khrestchatisky M., Heeren M.A., et al. Isolation and cloning of a voltage-dependent anion channel-like Mr 36,000 polypeptide from mammalian brain. J. Biol. Chem. 25:8679-8684, 1992.
26. Forst D., Schuelein K., Wacker T., et al. Crystallization and preliminary X-ray diffraction analysis of ScrY, a specific bacterial outer membrane porin. J. Mol. Biol. 229:258-262, 1993.
27. Forst D., Welte W., Wacker T., Diederichs K. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nature Struct. Biol. 5:37-46, 1998.
28. Thinnes F.P., Gotz H., Kayser H., et al. Identification of human porins. I. Purification of a porin from human B-lymphocytes (porin 31HL) and the topochemical proof of its expression on the plasmalemma of the progenitor cell. Biol. Chem. Hoppe-Seyler 370:1253-1264, 1989.
29. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685, 1970.
30. Schägger H., Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199:223-231, 1991.
31. Yvon M., Chabanet C., Pelissier J.P. Solubility of peptides in trichloroacetic acid (TCA) solutions. Hypothesis on the precipitation mechanism. Int. J. Pept. Protein Res. 34:166-176, 1989.
32. Bühler S., Schnaible V., Glocker M.O., et al. Conformational differentiation of two porin forms by selective chemical modification and MALDI-MS. In: Proceedings of the 14th IMSC, 1997, Tampere, Finland. in press.
33. Schiltz E., Kreusch A., Nestel U., Schulz G.E. Primary structure of porin from Rhodobacter capsulatus. Eur. J. Biochem. 199:587-594, 1991.
34. Kreusch A., Weiss M.S., Welte W., Weckesser J., Schulz G.E. Crystals of an integral membrane protein diffracting to 1.8 A resolution. J. Mol. Biol. 217:9-10, 1991.
35. Woitzik D., Weckesser J., Porin of Rhodobacter capsulatus: biochemical and functional characterisation. Z. Naturforsch. 45:576-582, 1990.
36. Shinohara Y., Kamida M., Yamazaki N., Terada H. Isolation and characterization of cDNA clones and a genetic clone encoding rat mitochondrial adenine nucleotide translocator. Biochim. Biophys. Acta 1152:192-196, 1993.
37. Beutner G., Rück A., Riede B., Brdiczka D. Complexes between hexokinase, mitochondrial porin and adenylate translocator in brain: regulation of hexokinase, oxidative phosphorylation and permeability transition pore. Biochem. Soc. Trans. 25:151-157, 1997.
38. Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:850-858, 1996.
39. Schuhmacher M., Glocker M.O., Wunderlin M., Przybylski M. Direct isolation of proteins from sodium dodecyl sulfate-polyacrylamide gel electrophoresis and analysis by electrospray-ionization mass spectrometry. Electrophoresis 17: 848-854, 1996.