메뉴 건너뛰기




Volumn 18, Issue 8, 1999, Pages 2084-2091

Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases

Author keywords

Cysteine; Endoplasmic reticulum; Multiple sulfatase deficiency; Protein modification; Sulfatase

Indexed keywords

ARGININE; ARYLSULFATASE; CYSTEINE; GLYCINE DERIVATIVE; POLYPEPTIDE; PROLINE; SERINE; SULFATASE; THREONINE;

EID: 0033561117     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.8.2084     Document Type: Article
Times cited : (129)

References (27)
  • 1
    • 0027424659 scopus 로고
    • Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class !-binding peptide into the endoplasmic reticulum in an ATP-dependent manner
    • Androlewicz, M.J., Anderson, K.S. and Cresswell, P. (1993) Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class !-binding peptide into the endoplasmic reticulum in an ATP-dependent manner. Proc. Natl Acad. Sci. USA, 90, 9130-9134.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9130-9134
    • Androlewicz, M.J.1    Anderson, K.S.2    Cresswell, P.3
  • 3
    • 12644318785 scopus 로고    scopus 로고
    • A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum
    • Dierks, T. et al. (1996) A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum. EMBO J., 15, 6931-6942.
    • (1996) EMBO J. , vol.15 , pp. 6931-6942
    • Dierks, T.1
  • 4
    • 0030711751 scopus 로고    scopus 로고
    • Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum
    • Dierks, T., Schmidt, B. and von Figura, K. (1997) Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Proc. Natl Acad. Sci. USA, 94, 11963-11968.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11963-11968
    • Dierks, T.1    Schmidt, B.2    Von Figura, K.3
  • 5
    • 0032475864 scopus 로고    scopus 로고
    • Formation of formylglycine in prokaryotic sulfatases by oxidation of either cysteine or serine
    • Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M.A. and von Figura, K. (1998a) Formation of formylglycine in prokaryotic sulfatases by oxidation of either cysteine or serine. J. Biol. Chem., 273, 25560-25564.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25560-25564
    • Dierks, T.1    Miech, C.2    Hummerjohann, J.3    Schmidt, B.4    Kertesz, M.A.5    Von Figura, K.6
  • 6
    • 0032512813 scopus 로고    scopus 로고
    • Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum
    • Dierks, T., Lecca, M.R., Schmidt, B. and von Figura, K. (1998b) Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS Lett., 423, 61-65.
    • (1998) FEBS Lett. , vol.423 , pp. 61-65
    • Dierks, T.1    Lecca, M.R.2    Schmidt, B.3    Von Figura, K.4
  • 7
    • 0029860204 scopus 로고    scopus 로고
    • Identification, characterization, and cloning of a phosphonate monoester hydrolase from Burkholderia caryophilli PG2982
    • Dotson, S.,B., Smith, C.E., Ling, C.S., Barry, G.F. and Kishore, G.M. (1996) Identification, characterization, and cloning of a phosphonate monoester hydrolase from Burkholderia caryophilli PG2982. J. Biol. Chem., 271, 25754-25761.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25754-25761
    • Dotson, S.B.1    Smith, C.E.2    Ling, C.S.3    Barry, G.F.4    Kishore, G.M.5
  • 8
    • 0031895566 scopus 로고    scopus 로고
    • New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling
    • Duret, L., Guex, N., Peitsch, M.C. and Bairoch, A. (1998) New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling. Genome Res., 8, 348-353.
    • (1998) Genome Res. , vol.8 , pp. 348-353
    • Duret, L.1    Guex, N.2    Peitsch, M.C.3    Bairoch, A.4
  • 9
    • 0028924667 scopus 로고
    • A cluster of sulfatase genes on Xp22.3: Mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy
    • Franco, B. et al. (1995) A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell, 81, 15-25.
    • (1995) Cell , vol.81 , pp. 15-25
    • Franco, B.1
  • 10
    • 0032491196 scopus 로고    scopus 로고
    • Residues critical for formylglycine formation and/or catalytic activity of arylsulfatase A
    • Knaust, A., Schmidt, B., Dierks, T., von Bülow, R. and von Figura, K. (1998) Residues critical for formylglycine formation and/or catalytic activity of arylsulfatase A. Biochemistry, 37, 13941-13946.
    • (1998) Biochemistry , vol.37 , pp. 13941-13946
    • Knaust, A.1    Schmidt, B.2    Dierks, T.3    Von Bülow, R.4    Von Figura, K.5
  • 11
    • 0001245698 scopus 로고
    • Metachromatic leukodystrophy and multiple sulfatase deficiency: Sulfatide lipidosis
    • Scriver, C.R., Beaudet, A.L., Sly, W.S. and Valle, D. (eds), McGraw-Hill, New York
    • Kolodny, E.H. and Fluharty, A.L. (1995) Metachromatic leukodystrophy and multiple sulfatase deficiency: sulfatide lipidosis. In Scriver, C.R., Beaudet, A.L., Sly, W.S. and Valle, D. (eds), The Metabolic and Molecular Bases of Inherited Disease. McGraw-Hill, New York, pp. 2693-2741.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 2693-2741
    • Kolodny, E.H.1    Fluharty, A.L.2
  • 12
    • 0032539976 scopus 로고    scopus 로고
    • Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis
    • Lukatela, G., Krauss, N., Theis, K., Selmer, T., Gieselmann, V., von Figura, K. and Saenger, W. (1998) Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry, 37, 3654-3664.
    • (1998) Biochemistry , vol.37 , pp. 3654-3664
    • Lukatela, G.1    Krauss, N.2    Theis, K.3    Selmer, T.4    Gieselmann, V.5    Von Figura, K.6    Saenger, W.7
  • 13
    • 0032570561 scopus 로고    scopus 로고
    • Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine
    • Miech, C., Dierks, T., Selmer, T., von Figura, K. and Schmidt, B. (1998) Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. J. Biol. Chem., 273, 4835-4837.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4835-4837
    • Miech, C.1    Dierks, T.2    Selmer, T.3    Von Figura, K.4    Schmidt, B.5
  • 14
    • 0027239749 scopus 로고
    • Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
    • Neefjes, J.J., Momburg, F. and Hammerling, G.J. (1993) Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science, 261, 769-771.
    • (1993) Science , vol.261 , pp. 769-771
    • Neefjes, J.J.1    Momburg, F.2    Hammerling, G.J.3
  • 15
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Brunak, S. and von Heijne, G. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engng, 10, 1-6.
    • (1997) Protein Engng , vol.10 , pp. 1-6
    • Nielsen, H.1    Brunak, S.2    Von Heijne, G.3
  • 17
    • 0032513051 scopus 로고    scopus 로고
    • Sulfatases: Trapping of the sulfated enzyme intermediate by substituting the active site formylglycine
    • Recksiek, M., Selmer, T., Dierks, T., Schmidt, B. and von Figura, K. (1998) Sulfatases: trapping of the sulfated enzyme intermediate by substituting the active site formylglycine. J. Biol. Chem., 273, 6096-6103.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6096-6103
    • Recksiek, M.1    Selmer, T.2    Dierks, T.3    Schmidt, B.4    Von Figura, K.5
  • 18
    • 0032145321 scopus 로고    scopus 로고
    • Computational analysis of bacterial sulfatases and their modifying enzymes
    • Schirmer, A. and Kolter, R. (1998) Computational analysis of bacterial sulfatases and their modifying enzymes. Chem. Biol., 5, R181-R186.
    • (1998) Chem. Biol. , vol.5
    • Schirmer, A.1    Kolter, R.2
  • 19
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt, B., Selmer, T., Ingendoh, A. and von Figura, K. (1995) A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell, 82, 271-278.
    • (1995) Cell , vol.82 , pp. 271-278
    • Schmidt, B.1    Selmer, T.2    Ingendoh, A.3    Von Figura, K.4
  • 20
    • 0029898602 scopus 로고    scopus 로고
    • The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri
    • Selmer, T., Hallmann, A., Schmidt, B., Sumper, M. and von Figura, K. (1996) The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. Eur. J. Biochem., 238, 341-345.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 341-345
    • Selmer, T.1    Hallmann, A.2    Schmidt, B.3    Sumper, M.4    Von Figura, K.5
  • 23
    • 0032986085 scopus 로고    scopus 로고
    • The iron sulfur protein AtsB is required for post-translational formation of formylglycin in the Klebsiella sulfatase
    • in press
    • Szameit, C., Miech, C., Balleininger, M., Schmidt, B., von Figura, K. and Dierks, T. (1999) The iron sulfur protein AtsB is required for post-translational formation of formylglycin in the Klebsiella sulfatase. J. Biol. Chem., 274, in press.
    • (1999) J. Biol. Chem. , vol.274
    • Szameit, C.1    Miech, C.2    Balleininger, M.3    Schmidt, B.4    Von Figura, K.5    Dierks, T.6
  • 24
    • 0032104543 scopus 로고    scopus 로고
    • A novel protein modification generating an aldehyde group in sulfatases: Its role in catalysis and disease
    • von Figura, K., Schmidt, B., Selmer, T. and Dierks, T. (1998) A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease. BioEssays, 20, 505-510.
    • (1998) BioEssays , vol.20 , pp. 505-510
    • Von Figura, K.1    Schmidt, B.2    Selmer, T.3    Dierks, T.4
  • 25
    • 0033617217 scopus 로고    scopus 로고
    • Amino acid residues forming the active site of arylsulfatase A: Role in catalytic activity and substrate binding
    • in press
    • Waldow, A., Schmidt, B., Dierks, T., von Bülow, R. and von Figura, K. (1999) Amino acid residues forming the active site of arylsulfatase A: role in catalytic activity and substrate binding. J. Biol. Chem., 274, in press.
    • (1999) J. Biol. Chem. , vol.274
    • Waldow, A.1    Schmidt, B.2    Dierks, T.3    Von Bülow, R.4    Von Figura, K.5
  • 26
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P. and Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol., 96, 84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 27
    • 0029121406 scopus 로고
    • Diversity of T cell receptor 8-chain cDNA in the thymus of a one-month-old pig
    • Yang, Y.G., Ohta, S., Yamada,S., Shimizu, M. and Takagaki, Y. (1995) Diversity of T cell receptor 8-chain cDNA in the thymus of a one-month-old pig. J. Immunol., 155, 1981-1993.
    • (1995) J. Immunol. , vol.155 , pp. 1981-1993
    • Yang, Y.G.1    Ohta, S.2    Shimizu, M.3    Takagaki, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.