메뉴 건너뛰기




Volumn 316, Issue 1-2, 2003, Pages 47-56

The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes

Author keywords

DUF323; Formylglycine generating enzyme; Multiple sulfatase deficiency; Sulfatase gene family; Sulfatase modifying factor

Indexed keywords

BIOLOGICAL FACTOR; CYSTEINE; GLYCINE DERIVATIVE; SULFATASE MODIFYING FACTOR 1; UNCLASSIFIED DRUG;

EID: 0141922853     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(03)00746-7     Document Type: Article
Times cited : (63)

References (36)
  • 2
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res. 28:2000;45-48.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 3
    • 0034987576 scopus 로고    scopus 로고
    • 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family
    • Boltes I., Czapinska H., Kahnert A., von Bülow R., Dierks T., Schmidt B., von Figura K., Kertesz M., Usón I. 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. Structure. 9:2001;483-491.
    • (2001) Structure , vol.9 , pp. 483-491
    • Boltes, I.1    Czapinska, H.2    Kahnert, A.3    Von Bülow, R.4    Dierks, T.5    Schmidt, B.6    Von Figura, K.7    Kertesz, M.8    Usón, I.9
  • 5
    • 0037509873 scopus 로고    scopus 로고
    • The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases
    • Cosma M., Pepe S., Annunziata I., Newbold R., Grompe M., Parenti G. The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases. Cell. 113:2003;445-456.
    • (2003) Cell , vol.113 , pp. 445-456
    • Cosma, M.1    Pepe, S.2    Annunziata, I.3    Newbold, R.4    Grompe, M.5    Parenti, G.6
  • 6
    • 0030711751 scopus 로고    scopus 로고
    • Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum
    • Dierks T., Schmidt B., von Figura K. Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 94:1997;11963-11968.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11963-11968
    • Dierks, T.1    Schmidt, B.2    Von Figura, K.3
  • 7
    • 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., Schmidt B., von Figura K. Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS Lett. 423:1998;61-65.
    • (1998) FEBS Lett. , vol.423 , pp. 61-65
    • Dierks, T.1    Lecca, M.2    Schmidt, B.3    Von Figura, K.4
  • 8
    • 0032475864 scopus 로고    scopus 로고
    • Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine
    • Dierks T., Miech C., Schmidt B., Kertesz M., von Figura K. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273:1998;25560-25564.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25560-25564
    • Dierks, T.1    Miech, C.2    Schmidt, B.3    Kertesz, M.4    Von Figura, K.5
  • 9
    • 0033561117 scopus 로고    scopus 로고
    • Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases
    • Dierks T., Lecca M., Schlotterhose P., Schmidt B., von Figura K. Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases. EMBO J. 18:1999;2084-2091.
    • (1999) EMBO J. , vol.18 , pp. 2084-2091
    • Dierks, T.1    Lecca, M.2    Schlotterhose, P.3    Schmidt, B.4    Von Figura, K.5
  • 11
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta R., Brunak S. Prediction of glycosylation across the human proteome and the correlation to protein function. Pac. Symp. Biocomput. 2002;310-322.
    • (2002) Pac. Symp. Biocomput. , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 12
    • 0034816908 scopus 로고    scopus 로고
    • Characterisation of nirV and a gene encoding a novel pseudoazurin in Rhodobacter sphaeroides 2.4.3
    • Jain R., Shapleigh J. Characterisation of nirV and a gene encoding a novel pseudoazurin in Rhodobacter sphaeroides 2.4.3. Microbiology. 147:2001;2505-2515.
    • (2001) Microbiology , vol.147 , pp. 2505-2515
    • Jain, R.1    Shapleigh, J.2
  • 13
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:1999;195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.1
  • 14
    • 0034713902 scopus 로고    scopus 로고
    • Site-directed mutagenesis and biochemical analysis of the endogenous ligands in the ferrous active site of clavaminate synthase. The His-3 variant of the 2-His-1-carboxylate model
    • Khaleeli N., Busby R., Townsend C. Site-directed mutagenesis and biochemical analysis of the endogenous ligands in the ferrous active site of clavaminate synthase. The His-3 variant of the 2-His-1-carboxylate model. Biochemistry. 39:2000;8666-8673.
    • (2000) Biochemistry , vol.39 , pp. 8666-8673
    • Khaleeli, N.1    Busby, R.2    Townsend, C.3
  • 15
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 16
    • 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., Saenger W. 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. 37:1998;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
  • 17
    • 0037462751 scopus 로고    scopus 로고
    • Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB
    • Marquordt C., Fang Q., Will E., Peng J., von Figura K., Dierks T. Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB. J. Biol. Chem. 278:2003;2212-2218.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2212-2218
    • Marquordt, C.1    Fang, Q.2    Will, E.3    Peng, J.4    Von Figura, K.5    Dierks, T.6
  • 18
    • 0029805240 scopus 로고    scopus 로고
    • Analysis of bacterial carbapenem antibiotic production genes reveals a novel beta-lactam biosynthesis pathway
    • McGowan S., Sebaihia M., Porter L., Stewart G., Williams P., Bycroft B., Salmond G. Analysis of bacterial carbapenem antibiotic production genes reveals a novel beta-lactam biosynthesis pathway. Mol. Microbiol. 22:1996;415-426.
    • (1996) Mol. Microbiol. , vol.22 , pp. 415-426
    • McGowan, S.1    Sebaihia, M.2    Porter, L.3    Stewart, G.4    Williams, P.5    Bycroft, B.6    Salmond, G.7
  • 19
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L., Bryson K., Jones D. The PSIPRED protein structure prediction server. Bioinformatics. 16:2000;404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.1    Bryson, K.2    Jones, D.3
  • 20
    • 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., Schmidt B. Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. J. Biol. Chem. 273:1998;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
  • 22
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 23
    • 0029853148 scopus 로고    scopus 로고
    • WWW-Query: An on-line retrieval system for biological sequence banks
    • Perriere G., Gouy M. WWW-Query: an on-line retrieval system for biological sequence banks. Biochimie. 78:1996;364-369.
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perriere, G.1    Gouy, M.2
  • 24
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European molecular biology open software suite
    • Rice P., Longden I., Bleasby A. EMBOSS: the European molecular biology open software suite. Trends Genet. 16:2000;276-277.
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 25
    • 0035910178 scopus 로고    scopus 로고
    • Transcriptional regulation of pentose utilisation systems in the Bacillus/Clostridium group of bacteria
    • Rodionov D., Mironov A., Gelfand M.S. Transcriptional regulation of pentose utilisation systems in the Bacillus/Clostridium group of bacteria. FEMS Microbiol. Lett. 205:2001;305-314.
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 305-314
    • Rodionov, D.1    Mironov, A.2    Gelfand, M.S.3
  • 27
    • 0032145321 scopus 로고    scopus 로고
    • Computational analysis of bacterial sulfatases and their modifying enzymes
    • Schirmer A., Kolter R. Computational analysis of bacterial sulfatases and their modifying enzymes. Chem. Biol. 5:1998;R181-R186.
    • (1998) Chem. Biol. , vol.5
    • Schirmer, A.1    Kolter, R.2
  • 28
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt B., Selmer T., Ingendoh A., von Figura K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 82:1995;271-278.
    • (1995) Cell , vol.82 , pp. 271-278
    • Schmidt, B.1    Selmer, T.2    Ingendoh, A.3    Von Figura, K.4
  • 30
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies
    • Strimmer K., von Haeseler A. Quartet puzzling: a quartet maximum likelihood method for reconstructing tree topologies. Mol. Biol. Evol. 13:1996;964-969.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 31
    • 0032986085 scopus 로고    scopus 로고
    • The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase
    • Szameit C., Miech C., Balleininger M., Schmidt B., von Figura K., Dierks T. The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. J. Biol. Chem. 274:1999;15375-15381.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15375-15381
    • Szameit, C.1    Miech, C.2    Balleininger, M.3    Schmidt, B.4    Von Figura, K.5    Dierks, T.6
  • 32
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J., Higgins D., Gibson T. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 33
    • 0035847029 scopus 로고    scopus 로고
    • Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis
    • von Bülow R., Schmidt B., Dierks T., von Figura K., Usón I. Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis. J. Mol. Biol. 305:2001;269-277.
    • (2001) J. Mol. Biol. , vol.305 , pp. 269-277
    • Von Bülow, R.1    Schmidt, B.2    Dierks, T.3    Von Figura, K.4    Usón, I.5
  • 34
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:1986;4683.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683
    • Von Heijne, G.1
  • 36
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S., Goldman N. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18:2001;691-699.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.