메뉴 건너뛰기




Volumn 13, Issue 1, 2012, Pages

Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 84861945664     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-13-9     Document Type: Article
Times cited : (32)

References (35)
  • 1
    • 0032800014 scopus 로고    scopus 로고
    • A superfamily of archaeal, bacterial and eukaryotic proteins homologous to animal transglutaminases
    • 10.1110/ps.8.8.1714
    • A superfamily of archaeal, bacterial and eukaryotic proteins homologous to animal transglutaminases. Makorova KS, Aravind L, Koonin EV, Prot Sci 1999 8 1714 1719 10.1110/ps.8.8.1714
    • (1999) Prot Sci , vol.8 , pp. 1714-1719
    • Makorova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 2
    • 0021294803 scopus 로고
    • Transglutaminases
    • 10.1007/BF00240602 6143256
    • Transglutaminases. Lorand L, Conrad SM, Mol Cell Biochem 1984 58 9 35 10.1007/BF00240602 6143256
    • (1984) Mol Cell Biochem , vol.58 , pp. 9-35
    • Lorand, L.1    Conrad, S.M.2
  • 3
    • 0037066733 scopus 로고    scopus 로고
    • Site-directed mutagenesis study of S.cerevisiae peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation
    • 10.1074/jbc.M111383200 11812789
    • Site-directed mutagenesis study of S.cerevisiae peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation. Katiyar S, Suzuki T, Balgobin BJ, Lennarz WJ, J Biol Chem 2002 277 12953 12959 10.1074/jbc.M111383200 11812789
    • (2002) J Biol Chem , vol.277 , pp. 12953-12959
    • Katiyar, S.1    Suzuki, T.2    Balgobin, B.J.3    Lennarz, W.J.4
  • 4
    • 0018116324 scopus 로고
    • Some characteristics of new glycopeptidase acting on aspartylglycosylamine linkages
    • 738997
    • Some characteristics of new glycopeptidase acting on aspartylglycosylamine linkages. Takahashi N, Nishibe H, J Biochem 1978 84 1467 1473 738997
    • (1978) J Biochem , vol.84 , pp. 1467-1473
    • Takahashi, N.1    Nishibe, H.2
  • 5
    • 0019888484 scopus 로고
    • Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide:N-glycosidase
    • 7287707
    • Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide:N-glycosidase. Plummer TH, Tarentino AL, J Biol Chem 1981 256 10243 10246 7287707
    • (1981) J Biol Chem , vol.256 , pp. 10243-10246
    • Plummer, T.H.1    Tarentino, A.L.2
  • 6
    • 0021189137 scopus 로고
    • Demonstration of peptide:N-glycosidase F activity in endo-beta-N- acetylglucosaminidase F preparations
    • 6206060
    • Demonstration of peptide:N-glycosidase F activity in endo-beta-N- acetylglucosaminidase F preparations. Plummer TH, Elder JH, Alexander S, Phelan AW, Tarentino AL, J Biol Chem 1984 259 10700 10704 6206060
    • (1984) J Biol Chem , vol.259 , pp. 10700-10704
    • Plummer, T.H.1    Elder, J.H.2    Alexander, S.3    Phelan, A.W.4    Tarentino, A.L.5
  • 7
    • 0028926641 scopus 로고
    • Kinetic comparison of peptide:N-glycosidases F and A reveals several differences in substrate specificity
    • 10.1007/BF00731873
    • Kinetic comparison of peptide:N-glycosidases F and A reveals several differences in substrate specificity. Altmann F, Schweiszer S, Weber C, Glycoconjugate J 1995 12 84 93 10.1007/BF00731873
    • (1995) Glycoconjugate J , vol.12 , pp. 84-93
    • Altmann, F.1    Schweiszer, S.2    Weber, C.3
  • 8
    • 0025887531 scopus 로고
    • Peptide:N-glycosidase activity found in the early embryos of Oryzias latipes (Medaka fish) the first demonstration of the occurrence of 22 peptide:N-glycosidase in animal cells and its implication for the presence of a de-N- glycosylation system in living organisms
    • 1718990
    • Peptide:N-glycosidase activity found in the early embryos of Oryzias latipes (Medaka fish) The first demonstration of the occurrence of 22 peptide:N-glycosidase in animal cells and its implication for the presence of a de-N- glycosylation system in living organisms. Seko A, Kitajima K, Inoue Y, Inoue S, J Biol Chem 1991 266 22110 22114 1718990
    • (1991) J Biol Chem , vol.266 , pp. 22110-22114
    • Seko, A.1    Kitajima, K.2    Inoue, Y.3    Inoue, S.4
  • 9
    • 0032850389 scopus 로고    scopus 로고
    • Identification of two discrete peptide:N- glycanases in Oryzias latipes during embryogenesis
    • 10.1093/glycob/9.9.887
    • Identification of two discrete peptide:N- glycanases in Oryzias latipes during embryogenesis. Seko A, Kitajima K, Iwamatsu T, Inoue Y, Inoue S, Glycobiol 1999 9 887 895 10.1093/glycob/9.9.887
    • (1999) Glycobiol , vol.9 , pp. 887-895
    • Seko, A.1    Kitajima, K.2    Iwamatsu, T.3    Inoue, Y.4    Inoue, S.5
  • 10
    • 0027259262 scopus 로고
    • Identification of peptide:N-glycanase activity in mammalian derived cultured cells
    • 10.1006/bbrc.1993.1938 8352768
    • Identification of peptide:N-glycanase activity in mammalian derived cultured cells. Suzuki T, Seko A, Kitajima K, Inoue Y, Inoue S, Biochem Biophys Res Commun 1993 194 1124 1130 10.1006/bbrc.1993.1938 8352768
    • (1993) Biochem Biophys Res Commun , vol.194 , pp. 1124-1130
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 11
    • 0030926458 scopus 로고    scopus 로고
    • Site-specific de-N-glycosylation of diglycosylated ovalbumin in hen oviduct by endogenous peptide: N-glycanase as a quality control system for newly synthesized proteins
    • 10.1073/pnas.94.12.6244 9177202
    • Site-specific de-N-glycosylation of diglycosylated ovalbumin in hen oviduct by endogenous peptide: N-glycanase as a quality control system for newly synthesized proteins. Suzuki T, Kitajima K, Emori Y, Inoue Y, Inoue S, Proc Natl Acad Sci USA 1997 94 6244 6249 10.1073/pnas.94.12.6244 9177202
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6244-6249
    • Suzuki, T.1    Kitajima, K.2    Emori, Y.3    Inoue, Y.4    Inoue, S.5
  • 12
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of S. cerevisiae are subsequently deglycosylated by a soluble peptide: N-glycanase activity
    • 10.1074/jbc.273.34.21526 9705282
    • Peptides glycosylated in the endoplasmic reticulum of S. cerevisiae are subsequently deglycosylated by a soluble peptide: N-glycanase activity. Suzuki T, Park H, Kitajima K, Lennarz WJ, J Biol Chem 1998 273 21526 21530 10.1074/jbc.273.34.21526 9705282
    • (1998) J Biol Chem , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 14
    • 0028362217 scopus 로고
    • Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation
    • 8021270
    • Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation. Suzuki T, Seko A, Kitajima K, Inoue Y, Inoue S, J Biol Chem 1994 269 17611 17618 8021270
    • (1994) J Biol Chem , vol.269 , pp. 17611-17618
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 15
    • 78649325827 scopus 로고    scopus 로고
    • S. cerevisiae N-glycanase distinguishes between native and non-native glycoproteins
    • 10.1038/sj.embor.7400066 14726951
    • S. cerevisiae N-glycanase distinguishes between native and non-native glycoproteins. Hirsch C, Misaghi S, Blom D, Pacold ME, Ploegh HL, EMBO Rep 2004 5 201 206 10.1038/sj.embor.7400066 14726951
    • (2004) EMBO Rep , vol.5 , pp. 201-206
    • Hirsch, C.1    Misaghi, S.2    Blom, D.3    Pacold, M.E.4    Ploegh, H.L.5
  • 16
    • 0034729193 scopus 로고    scopus 로고
    • PNG1, a S. cerevisiae gene encoding a highly conserved peptide:N-glycanase
    • 10.1083/jcb.149.5.1039 10831608
    • PNG1, a S. cerevisiae gene encoding a highly conserved peptide:N-glycanase. Suzuki T, Park H, Hollingsworth NM, Sternglanz R, Lennarz WJ, J Cell Biol 2000 149 1039 1052 10.1083/jcb.149.5.1039 10831608
    • (2000) J Cell Biol , vol.149 , pp. 1039-1052
    • Suzuki, T.1    Park, H.2    Hollingsworth, N.M.3    Sternglanz, R.4    Lennarz, W.J.5
  • 17
    • 76149108805 scopus 로고    scopus 로고
    • The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans
    • 10.1523/JNEUROSCI.4962-08.2010 20130186
    • The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans. Habibi-Babadi N, Su A, de Carvalho CE, Colavita A, J Neurosci 2010 30 1766 1776 10.1523/JNEUROSCI.4962-08.2010 20130186
    • (2010) J Neurosci , vol.30 , pp. 1766-1776
    • Habibi-Babadi, N.1    Su, A.2    De Carvalho, C.E.3    Colavita, A.4
  • 18
    • 77449127431 scopus 로고    scopus 로고
    • The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity
    • 10.1074/jbc.M109.045302 19940117
    • The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity. Maerz S, Funakoshi Y, Negishi Y, Suzuki T, Seiler S, J Biol Chem 2010 285 2326 2332 10.1074/jbc.M109.045302 19940117
    • (2010) J Biol Chem , vol.285 , pp. 2326-2332
    • Maerz, S.1    Funakoshi, Y.2    Negishi, Y.3    Suzuki, T.4    Seiler, S.5
  • 19
    • 1542313957 scopus 로고    scopus 로고
    • Adenylyl cyclase G is activated by an intramolecular osmosensor
    • 14718564
    • Adenylyl cyclase G is activated by an intramolecular osmosensor. Saran S, Schaap P, Mol Biol Cell 2004 15 1479 1486 14718564
    • (2004) Mol Biol Cell , vol.15 , pp. 1479-1486
    • Saran, S.1    Schaap, P.2
  • 20
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling
    • 10.1093/bioinformatics/bti770 16301204
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Arnold K, Bordoli L, Kopp J, Schwede T, Bioinformatics 2006 22 195 201 10.1093/bioinformatics/bti770 16301204
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 21
    • 21544450264 scopus 로고    scopus 로고
    • Structure of a peptide: N-glycanase-Rad23 complex: Insight into the deglycosylation for denatured glycoproteins
    • 10.1073/pnas.0502082102 15964983
    • Structure of a peptide: N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins. Lee JH, Choi JM, Lee C, Yi KJ, Cho Y, Proc Natl Acad Sci USA 2005 102 9144 9149 10.1073/pnas.0502082102 15964983
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9144-9149
    • Lee, J.H.1    Choi, J.M.2    Lee, C.3    Yi, K.J.4    Cho, Y.5
  • 22
    • 33744962966 scopus 로고    scopus 로고
    • Structure of the mouse peptide:N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum- associated degradation and DNA repair pathways
    • 10.1074/jbc.M600137200 16500903
    • Structure of the mouse peptide:N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum- associated degradation and DNA repair pathways. Zhao G, Zhou X, Wang L, Li G, Kisker C, Lennarz WJ, Schindelin H, J Biol Chem 2006 281 13751 13761 10.1074/jbc.M600137200 16500903
    • (2006) J Biol Chem , vol.281 , pp. 13751-13761
    • Zhao, G.1    Zhou, X.2    Wang, L.3    Li, G.4    Kisker, C.5    Lennarz, W.J.6    Schindelin, H.7
  • 23
    • 33750122391 scopus 로고    scopus 로고
    • Investigating Gene Expression: In Situ Hybridization and Reporter Genes. Dictyostelium discoideum Protocols
    • 16957295
    • Investigating Gene Expression: In Situ Hybridization and Reporter Genes. Dictyostelium discoideum Protocols. Escalante R, Sastre L, Methods Mol Biol 2006 346 III 247 260 16957295
    • (2006) Methods Mol Biol , vol.346 , Issue.3 , pp. 247-260
    • Escalante, R.1    Sastre, L.2
  • 24
    • 0027217068 scopus 로고
    • A transformation vector for Dictyostelium discoideum with a new selectable marker Bsr
    • 10.1006/plas.1993.1042 8234487
    • A transformation vector for Dictyostelium discoideum with a new selectable marker Bsr. Sutoh K, Plasmid 1993 30 150 154 10.1006/plas.1993.1042 8234487
    • (1993) Plasmid , vol.30 , pp. 150-154
    • Sutoh, K.1
  • 25
    • 12744281810 scopus 로고    scopus 로고
    • Misfolding of glycoproteins is a prerequisite for peptide:N- glycanase mediated deglycosylation
    • 10.1016/j.febslet.2004.12.060 15670854
    • Misfolding of glycoproteins is a prerequisite for peptide:N- glycanase mediated deglycosylation. Joshi S, Katiyar S, Lennarz WJ, FEBS Lett 2005 579 823 826 10.1016/j.febslet.2004.12.060 15670854
    • (2005) FEBS Lett , vol.579 , pp. 823-826
    • Joshi, S.1    Katiyar, S.2    Lennarz, W.J.3
  • 26
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3 942051
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Bradford MM, Anal Biochem 1976 72 248 254 10.1016/0003-2697(76)90527-3 942051
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 35748935131 scopus 로고    scopus 로고
    • Unique Peptide:N-glycanase of Caenorhabditis elegans has activity of protein disulphide reductase as well as of deglycosylation
    • 10.1093/jb/mvm117 17522090
    • Unique Peptide:N-glycanase of Caenorhabditis elegans has activity of protein disulphide reductase as well as of deglycosylation. Kato T, Kawahara A, Ashida H, Yamamoto K, J Biochem 2007 142 175 181 10.1093/jb/mvm117 17522090
    • (2007) J Biochem , vol.142 , pp. 175-181
    • Kato, T.1    Kawahara, A.2    Ashida, H.3    Yamamoto, K.4
  • 28
    • 33751213902 scopus 로고    scopus 로고
    • Structural and biochemical studies of the C-terminal domain of mouse peptide:N-glycanase identify it as a mannose-binding module
    • 10.1073/pnas.0602954103 17088551
    • Structural and biochemical studies of the C-terminal domain of mouse peptide:N-glycanase identify it as a mannose-binding module. Zhou X, Zhao G, Truglio JJ, Wang L, Li G, Lennarz WJ, Schindelin H, Proc Natl Acad Sci USA 2006 103 17214 17219 10.1073/pnas.0602954103 17088551
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17214-17219
    • Zhou, X.1    Zhao, G.2    Truglio, J.J.3    Wang, L.4    Li, G.5    Lennarz, W.J.6    Schindelin, H.7
  • 29
    • 77949530204 scopus 로고    scopus 로고
    • N-Terminal Deletion of Peptide:N-Glycanase Results in Enhanced Deglycosylation Activity
    • 10.1371/journal.pone.0008335 20016784
    • N-Terminal Deletion of Peptide:N- Glycanase Results in Enhanced Deglycosylation Activity. Wang S, Xin S, Liu X, Wang Y, An Z, Peng QQ, Wang G, PLoS One 2009 4 8335 10.1371/journal.pone.0008335 20016784
    • (2009) PLoS One , vol.4 , pp. 58335
    • Wang, S.1    Xin, S.2    Liu, X.3    Wang, Y.4    An, Z.5    Peng, Q.Q.6    Wang, G.7
  • 31
    • 4644318292 scopus 로고    scopus 로고
    • A complex between peptide: N-glycanase and two proteosome- linked proteins suggests a mechanism for the degradation of misfolded glycoproteins
    • 10.1073/pnas.0405663101 15358861
    • A complex between peptide: N-glycanase and two proteosome- linked proteins suggests a mechanism for the degradation of misfolded glycoproteins. Katiyar S, Li G, Lennarz WJ, Proc Natl Acad Sci USA 2004 101 13774 13779 10.1073/pnas.0405663101 15358861
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13774-13779
    • Katiyar, S.1    Li, G.2    Lennarz, W.J.3
  • 32
    • 27644581602 scopus 로고    scopus 로고
    • Multiple modes of interaction of the deglycosylation enzyme, mouse peptide:N-glycanase, with the proteosome
    • 10.1073/pnas.0507155102 16249333
    • Multiple modes of interaction of the deglycosylation enzyme, mouse peptide:N-glycanase, with the proteosome. Li G, Zhou X, Zhao G, Schindelin H, Lennarz WJ, Proc Natl Acad Sci USA 2005 102 15809 15814 10.1073/pnas.0507155102 16249333
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15809-15814
    • Li, G.1    Zhou, X.2    Zhao, G.3    Schindelin, H.4    Lennarz, W.J.5
  • 33
    • 26244466567 scopus 로고    scopus 로고
    • The retrotranslocation protein Derlin-1 binds peptide: N- glycanase to the endoplasmic reticulum
    • 10.1091/mbc.E05-04-0345 16055502
    • The retrotranslocation protein Derlin-1 binds peptide: N- glycanase to the endoplasmic reticulum. Katiyar S, Joshi S, Lennarz WJ, Mol Biol Cell 2005 16 4584 4594 10.1091/mbc.E05-04-0345 16055502
    • (2005) Mol Biol Cell , vol.16 , pp. 4584-4594
    • Katiyar, S.1    Joshi, S.2    Lennarz, W.J.3
  • 34
    • 34748833562 scopus 로고    scopus 로고
    • The Arabidopsis AtPNG1 gene encodes a peptide:N-glycanase
    • 10.1111/j.1365-313X.2007.03215.x 17666024
    • The Arabidopsis AtPNG1 gene encodes a peptide:N-glycanase. Diepold A, Li G, Lennarz WJ, Nurnberger T, Brunner F, Plant J 2007 52 94 104 10.1111/j.1365-313X.2007.03215.x 17666024
    • (2007) Plant J , vol.52 , pp. 94-104
    • Diepold, A.1    Li, G.2    Lennarz, W.J.3    Nurnberger, T.4    Brunner, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.