Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme

Mariappan M, Preusser-Kunze A, Balleininger M, Eiselt N, Schmidt B, Gande SL, Wenzel D, Dierks T, Figura von K (2005)
JOURNAL OF BIOLOGICAL CHEMISTRY 280(15): 15173-15179.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Mariappan, M; Preusser-Kunze, A; Balleininger, M; Eiselt, N; Schmidt, B; Gande, SL; Wenzel, D; Dierks, ThomasUniBi; Figura von, K
Abstract / Bemerkung
pFGE is the paralog of the formylglycine-generating enzyme (FGE), which catalyzes the oxidation of a specific cysteine to C alpha-formylglycine, the catalytic residue in the active site of sulfatases. The enzymatic activity of sulfatases depends on this posttranslational modification, and the genetic defect of FGE causes multiple sulfatase deficiency. The structural and functional properties of pFGE were analyzed. The comparison with FGE demonstrates that both share a tissue-specific expression pattern and the localization in the lumen of the endoplasmic reticulum. Both are retained in the endoplasmic reticulum by a saturable mechanism. Limited proteolytic cleavage at similar sites indicates that both also share a similar three-dimensional structure. pFGE, however, is lacking the formylglycine-generating activity of FGE. Although overexpression of FGE stimulates the generation of catalytically active sulfatases, overexpression of pFGE has an inhibitory effect. In vitro pFGE interacts with sulfatase-derived peptides but not with FGE. The inhibitory effect of pFGE on the generation of active sulfatases may therefore be caused by a competition of pFGE and FGE for newly synthesized sulfatase polypeptides.
Erscheinungsjahr
2005
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
280
Ausgabe
15
Seite(n)
15173-15179
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/2350712

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Mariappan M, Preusser-Kunze A, Balleininger M, et al. Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY. 2005;280(15):15173-15179.
Mariappan, M., Preusser-Kunze, A., Balleininger, M., Eiselt, N., Schmidt, B., Gande, S. L., Wenzel, D., et al. (2005). Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY, 280(15), 15173-15179. https://doi.org/10.1074/jbc.M413698200
Mariappan, M, Preusser-Kunze, A, Balleininger, M, Eiselt, N, Schmidt, B, Gande, SL, Wenzel, D, Dierks, Thomas, and Figura von, K. 2005. “Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme”. JOURNAL OF BIOLOGICAL CHEMISTRY 280 (15): 15173-15179.
Mariappan, M., Preusser-Kunze, A., Balleininger, M., Eiselt, N., Schmidt, B., Gande, S. L., Wenzel, D., Dierks, T., and Figura von, K. (2005). Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY 280, 15173-15179.
Mariappan, M., et al., 2005. Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY, 280(15), p 15173-15179.
M. Mariappan, et al., “Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 280, 2005, pp. 15173-15179.
Mariappan, M., Preusser-Kunze, A., Balleininger, M., Eiselt, N., Schmidt, B., Gande, S.L., Wenzel, D., Dierks, T., Figura von, K.: Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY. 280, 15173-15179 (2005).
Mariappan, M, Preusser-Kunze, A, Balleininger, M, Eiselt, N, Schmidt, B, Gande, SL, Wenzel, D, Dierks, Thomas, and Figura von, K. “Expression, localization, structural, and functional characterization of pFGE, the paralog of the C alpha-formylglycine-generating enzyme”. JOURNAL OF BIOLOGICAL CHEMISTRY 280.15 (2005): 15173-15179.

14 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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Proprotein convertases process and thereby inactivate formylglycine-generating enzyme.
Ennemann EC, Radhakrishnan K, Mariappan M, Wachs M, Pringle TH, Schmidt B, Dierks T., J Biol Chem 288(8), 2013
PMID: 23288839
HpSumf1 is involved in the activation of sulfatases responsible for regulation of skeletogenesis during sea urchin development.
Sakuma T, Ohnishi K, Fujita K, Ochiai H, Sakamoto N, Yamamoto T., Dev Genes Evol 221(3), 2011
PMID: 21706447
Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals.
Gande SL, Mariappan M, Schmidt B, Pringle TH, von Figura K, Dierks T., FEBS J 275(6), 2008
PMID: 18266766
Sulfotransferases, sulfatases and formylglycine-generating enzymes: a sulfation fascination.
Bojarová P, Williams SJ., Curr Opin Chem Biol 12(5), 2008
PMID: 18625336
A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.
Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG., Proc Natl Acad Sci U S A 103(1), 2006
PMID: 16368756
Identification of sites of mannose 6-phosphorylation on lysosomal proteins.
Sleat DE, Zheng H, Qian M, Lobel P., Mol Cell Proteomics 5(4), 2006
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Diez-Roux G, Ballabio A., Annu Rev Genomics Hum Genet 6(), 2005
PMID: 16124866
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
Dierks T, Dickmanns A, Preusser-Kunze A, Schmidt B, Mariappan M, von Figura K, Ficner R, Rudolph MG., Cell 121(4), 2005
PMID: 15907468

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