Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp

Molecular Biology of the Cell

Volumn 9, Issue 2, 1998, Pages 301-309

  Krieg, Joachim ^a   Hartmann, Steffen ^a   Vicentini, Anna ^a   Gläsner, Wolfgang ^a   Hess, Daniel ^a   Hofsteenge, Jan ^a  

^a FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CHIMERIC PROTEIN; MANNOSE; RECOMBINANT INTERLEUKIN 12; RIBONUCLEASE; TRYPTOPHAN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DATA BASE; DELETION MUTANT; ENZYME GLYCOSYLATION; ENZYME STRUCTURE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

MAMMALIA; TRIXIS;

EID: 0031882332     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.2.301     Document Type: Article

References (23)

1. Baranski, T.J., Faust, P.L., and Kornfeld, S. (1990). Generation of a lysosomal targeting signal in the secretory protein pepsinogen. Cell 63, 281-291.
2. Baranski, T.J., Koelsch, G., Hartsuck, J.A., and Kornfeld, S. (1991). Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting. J. Biol. Chem. 266, 23365-23372.
3. Beintema, J.J., Hofsteenge, J., Iwama, M., Morita, T., Ohgi, K., Irie, M., Sugiyama, R.H., Schieven, G.L., Dekker, C.A., and Glitz, D.G. (1988). Amino acid sequence of the nonsecretory ribonuclease of human urine. Biochemistry 27, 4530-4538.
4. Bergwerff, A.A., Oostrum, J., Asselbergs, A.M., Buergi, R., Hokke, H., Kamerling, J.P., and Vliegenthart, F.G. (1993). Primary structure of N-linked carbohydrate chains of a human chimeric plasminogen activator K2tu-PA expressed in Chinese hamster ovary cells. Eur. J. Biochem. 212, 639-656.
5. de Beer, T., Vliegenthart, J.F.G., Löffler, A., and Hofsteenge, J. (1995). The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is α-mannopyranose. Biochemistry 34, 11785-11789.
6. Doucey, M.-A., Hess, D., Cacan, R., and Hofsteenge, J. (1998). Protein C-mannosylation is enzyme-catalyzed and uses dolichyl-phosphate-mannose as a precursor. Mol. Biol. Cell 9, 291-300.
7. Durack, D.T., Ackerman, S.J., Loegering, D.A., and Gleich, G.J. (1981). Purification of human eosinophil-derived neurotoxin. Proc. Natl. Acad. Sci. USA 78, 5165-5169.
8. Durack, D.T., Sumi, S.M., and Klebanoff, S.J. (1979). Neurotoxicity of human eosinophils. Proc. Natl. Acad. Sci. USA 76, 1443-1447.
9. Gordon, M.H. (1933). Remarks on Hodgkin's disease. Br. Med. J. 1, 641-644.
10. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., and Pease, L.R. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
11. Hofsteenge, J., Müller, D.R., de Beer, T., Löffler, A., Richter, W.J., and Vliegenthart, J.F.G. (1994). New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us. Biochemistry 33, 13524-13530.
12. Irie, M., Nitta, R., Ohgi, K., Niwata, Y., Watanabe, H., Iwama, M., Beintema, J.J., Sanda, A., and Takizawa, Y. (1988). Primary structure of a non-secretory ribonuclease from bovine kidney. J. Biochem. 104, 289-296.
13. Iwama, M., Sanda, A., Ohgi, K., Hofsteenge, J., and Irie, M. (1993). Purification and primary structure of a porcine kidney non-secretory ribonuclease. Biosci. Biotech. Biochem. 57, 2133-2138.
14. Krieg, J., Gläsner, W., Vicentini, A., Doucey, M.-A., Löffler, A., Hess, D., and Hofsteenge, J. (1997). Protein C-mannosylation is an intra-cellular process performed by a variety of cultured cells. J. Biol. Chem. 272, 26687-26692.
15. Löffler, A., Doucey, M.-A., Jansson, A.M., Müller, D.R., de Beer, T., Hess, D., Meldal, M., Richter, W.J., Vliegenthart, J.F.G., and Hofsteenge, J. (1996). Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms. Biochemistry 35, 12005-12014.
16. Mosimann, S.C., Newton, D.L., Youle, R.J., and James, M.N.G. (1996). X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 Å resolution. J. Mol. Biol. 260, 540-552.
17. Pisano, A., Redmond, J.W., Williams, K.L., and Gooley, A.A. (1993). Glycosylation sites identified by solid-phase edman degradation: O-linked glycosylation motifs on human glycophorin A. Glycobiology 3, 429-435.
18. Reitman, M.L., and Kornfeld, S. (1985). Lysosomal enzyme targeting. J. Biol. Chem. 256, 11977-11980.
19. Rosenberg, H.F., Tenen, D.G., and Ackerman, S.J. (1989). Molecular cloning of the human eosinophil-derived neurotoxin:A member of the ribonuclease gene family. Proc. Natl. Acad. Sci. USA 86, 4460-4464.
20. Rosenberg, H.F., Dyer, K.D., Tiffany, H.L., and Gonzalez, M. (1995). Rapid evolution of a unique family of primate ribonuclease genes. Nat. Genet. 10, 219-223.
21. Sanger, F., Nicklen, S., and Coulson, A.R. (1977). DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
22. Vicentini, A., Hemmings, B.A., and Hofsteenge, J. (1994). Residues 36-42 of liver RNase PL3 contribute to its uridine-preferring substrate specificity. Protein Sci. 3, 459-466.
23. Wilm, M., and Mann, M. (1996). Analytical properties of the nanoelectrospray ion source. Anal. Chem. 68, 1-8.