메뉴 건너뛰기




Volumn 346, Issue 5, 2005, Pages 1275-1286

Analysis of human Pex19p's domain structure by pentapeptide scanning mutagenesis

Author keywords

Biogenesis; Peroxisomes; Pex19p; Protein import; Transposon mutagenesis

Indexed keywords

CHAPERONE; MEMBRANE PROTEIN; PENTAPEPTIDE; PEROXIN; PEROXIN 11; PEROXIN 12; PEROXIN 13; PEROXIN 14; PEROXIN 16; PEROXIN 19; PEROXIN 26; PEROXIN 3; PEROXIN 5; UNCLASSIFIED DRUG;

EID: 13844281618     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.013     Document Type: Article
Times cited : (54)

References (45)
  • 2
    • 2142697998 scopus 로고    scopus 로고
    • Metabolic and molecular basis of peroxisomal disorders: A review
    • R.J. Wanders Metabolic and molecular basis of peroxisomal disorders: a review Am. J. Med. Genet. 126 2004 355 375
    • (2004) Am. J. Med. Genet. , vol.126 , pp. 355-375
    • Wanders, R.J.1
  • 5
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes
    • N. Matsumoto, S. Tamura, and Y. Fujiki The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes Nature Cell Biol. 5 2003 454 460
    • (2003) Nature Cell Biol. , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3
  • 6
    • 0034208172 scopus 로고    scopus 로고
    • How peroxisomes arise
    • S.R. Terlecky, and M. Fransen How peroxisomes arise Traffic 1 2000 465 473
    • (2000) Traffic , vol.1 , pp. 465-473
    • Terlecky, S.R.1    Fransen, M.2
  • 7
    • 1842853027 scopus 로고    scopus 로고
    • Peroxisome biogenesis and the role of protein import
    • L.A. Brown, and A. Baker Peroxisome biogenesis and the role of protein import J. Cell. Mol. Med. 7 2003 388 400
    • (2003) J. Cell. Mol. Med. , vol.7 , pp. 388-400
    • Brown, L.A.1    Baker, A.2
  • 8
    • 3042695949 scopus 로고    scopus 로고
    • Peroxisome membrane biogenesis: The stage is set
    • W. Schliebs, and W.H. Kunau Peroxisome membrane biogenesis: the stage is set Curr. Biol. 14 2004 R397 R399
    • (2004) Curr. Biol. , vol.14
    • Schliebs, W.1    Kunau, W.H.2
  • 9
    • 7944224890 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes and glycosomes: Trypanosomatid glycosome assembly is a promising new drug target
    • J. Moyersoen, J. Choe, E. Fan, G.J. Hol, and P.A. Michels Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target FEMS Microbiol. Rev. 28 2004 603 643
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 603-643
    • Moyersoen, J.1    Choe, J.2    Fan, E.3    Hol, G.J.4    Michels, P.A.5
  • 10
    • 0028101960 scopus 로고
    • Sequence of a putative human housekeeping gene (HK33) localized on chromosome 1
    • A. Braun, S. Kammerer, W. Weissenhorn, E.H. Weiss, and H. Cleve Sequence of a putative human housekeeping gene (HK33) localized on chromosome 1 Gene 146 1994 291 295
    • (1994) Gene , vol.146 , pp. 291-295
    • Braun, A.1    Kammerer, S.2    Weissenhorn, W.3    Weiss, E.H.4    Cleve, H.5
  • 11
    • 0034641098 scopus 로고    scopus 로고
    • The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane
    • W.B. Snyder, A. Koller, A.J. Choy, and S. Subramani The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane J. Cell Biol. 149 1999 1171 1178
    • (1999) J. Cell Biol. , vol.149 , pp. 1171-1178
    • Snyder, W.B.1    Koller, A.2    Choy, A.J.3    Subramani, S.4
  • 12
    • 0034611003 scopus 로고    scopus 로고
    • PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis
    • K.A. Sacksteder, J.M. Jones, S.T. South, X. Li, Y. Liu, and S.J. Gould PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis J. Cell Biol. 148 2000 931 944
    • (2000) J. Cell Biol. , vol.148 , pp. 931-944
    • Sacksteder, K.A.1    Jones, J.M.2    South, S.T.3    Li, X.4    Liu, Y.5    Gould, S.J.6
  • 13
    • 0034728796 scopus 로고    scopus 로고
    • Human adrenoleukodystrophy protein and related peroxisomal ABC transporters interact with the peroxisomal assembly protein PEX19p
    • C.J. Gloeckner, P.U. Mayerhofer, P. Landgraf, A.C. Muntau, A. Holzinger, and J.K. Gerber Human adrenoleukodystrophy protein and related peroxisomal ABC transporters interact with the peroxisomal assembly protein PEX19p Biochem. Biophys. Res. Commun. 271 2000 144 150
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 144-150
    • Gloeckner, C.J.1    Mayerhofer, P.U.2    Landgraf, P.3    Muntau, A.C.4    Holzinger, A.5    Gerber, J.K.6
  • 14
    • 0034972812 scopus 로고    scopus 로고
    • Human Pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences
    • M. Fransen, T. Wylin, C. Brees, G.P. Mannaerts, and P.P. Van Veldhoven Human Pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences Mol. Cell. Biol. 21 2001 4413 4424
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4413-4424
    • Fransen, M.1    Wylin, T.2    Brees, C.3    Mannaerts, G.P.4    Van Veldhoven, P.P.5
  • 17
    • 0042130361 scopus 로고    scopus 로고
    • The interaction between human PEX3 and PEX19 characterized by fluorescence resonance energy transfer (FRET) analysis
    • A.C. Muntau, A.A. Roscher, W.H. Kunau, and G. Dodt The interaction between human PEX3 and PEX19 characterized by fluorescence resonance energy transfer (FRET) analysis Eur. J. Cell Biol. 82 2003 333 342
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 333-342
    • Muntau, A.C.1    Roscher, A.A.2    Kunau, W.H.3    Dodt, G.4
  • 18
    • 13044312086 scopus 로고    scopus 로고
    • Human PEX19: CDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome, and potential role in peroxisomal membrane assembly
    • Y. Matsuzono, N. Kinoshita, S. Tamura, N. Shimozawa, M. Hamasaki, and K. Ghaedi Human PEX19: cDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome, and potential role in peroxisomal membrane assembly Proc. Natl Acad. Sci. USA 96 1999 2116 2121
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2116-2121
    • Matsuzono, Y.1    Kinoshita, N.2    Tamura, S.3    Shimozawa, N.4    Hamasaki, M.5    Ghaedi, K.6
  • 19
    • 0032471958 scopus 로고    scopus 로고
    • Genetic basis of peroxisome-assembly mutants of humans. Chinese hamster ovary cells, and yeast: Identification of a new complementation group of peroxisome-biogenesis disorders apparently lacking peroxisomal-membrane ghosts
    • N. Shimozawa, Y. Suzuki, Z. Zhang, A. Imamura, N. Kondo, and N. Kinoshita Genetic basis of peroxisome-assembly mutants of humans. Chinese hamster ovary cells, and yeast: identification of a new complementation group of peroxisome-biogenesis disorders apparently lacking peroxisomal-membrane ghosts Am. J. Hum. Genet. 63 1998 1898 1903
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. 1898-1903
    • Shimozawa, N.1    Suzuki, Y.2    Zhang, Z.3    Imamura, A.4    Kondo, N.5    Kinoshita, N.6
  • 20
    • 0034677197 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins
    • E.H. Hettema, W. Girzalsky, M. van Den Berg, R. Erdmann, and B. Distel Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins EMBO J. 19 2000 223 233
    • (2000) EMBO J. , vol.19 , pp. 223-233
    • Hettema, E.H.1    Girzalsky, W.2    Van Den Berg, M.3    Erdmann, R.4    Distel, B.5
  • 21
    • 0345861756 scopus 로고    scopus 로고
    • PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
    • J.M. Jones, J.C. Morrell, and S.J. Gould PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins J. Cell Biol. 164 2004 57 67
    • (2004) J. Cell Biol. , vol.164 , pp. 57-67
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 22
    • 3042724871 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals
    • H. Rottensteiner, A. Kramer, S. Lorenzen, K. Stein, C. Landgraf, R. Volkmer-Engert, and R. Erdmann Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals Mol. Biol. Cell 15 2004 3406 3417
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3406-3417
    • Rottensteiner, H.1    Kramer, A.2    Lorenzen, S.3    Stein, K.4    Landgraf, C.5    Volkmer-Engert, R.6    Erdmann, R.7
  • 23
    • 0037016760 scopus 로고    scopus 로고
    • Two different targeting signals direct human peroxisomal membrane protein 22 to peroxisomes
    • U. Brosius, T. Dehmel, and J. Gartner Two different targeting signals direct human peroxisomal membrane protein 22 to peroxisomes J. Biol. Chem. 277 2002 774 784
    • (2002) J. Biol. Chem. , vol.277 , pp. 774-784
    • Brosius, U.1    Dehmel, T.2    Gartner, J.3
  • 24
    • 0034817401 scopus 로고    scopus 로고
    • Targeting elements in the amino-terminal part direct the human PMP70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes
    • M. Biermanns, and J. Gartner Targeting elements in the amino-terminal part direct the human PMP70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes Biochem. Biophys. Res. Commun. 285 2001 649 655
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 649-655
    • Biermanns, M.1    Gartner, J.2
  • 25
    • 0035196588 scopus 로고    scopus 로고
    • Yarrowia lipolytica cells mutant for the peroxisomal peroxin Pex19p contain structures resembling wild-type peroxisomes
    • G.R. Lambkin, and R.A. Rachubinski Yarrowia lipolytica cells mutant for the peroxisomal peroxin Pex19p contain structures resembling wild-type peroxisomes Mol. Biol. Cell 12 2001 3353 3364
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3353-3364
    • Lambkin, G.R.1    Rachubinski, R.A.2
  • 28
    • 0034548711 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Encouraging old proteins to execute unusual tricks
    • F. Hayes, and B. Hallet Pentapeptide scanning mutagenesis: encouraging old proteins to execute unusual tricks Trends Microbiol. 8 2000 571 577
    • (2000) Trends Microbiol. , vol.8 , pp. 571-577
    • Hayes, F.1    Hallet, B.2
  • 30
    • 0033015535 scopus 로고    scopus 로고
    • Pex19p interacts with Pex3p and Pex10p and is essential for peroxisome biogenesis in Pichia pastoris
    • W.B. Snyder, K.N. Faber, T.J. Wenzel, A. Koller, G.H. Luers, and L. Rangell Pex19p interacts with Pex3p and Pex10p and is essential for peroxisome biogenesis in Pichia pastoris Mol. Biol. Cell 10 1999 1745 1761
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1745-1761
    • Snyder, W.B.1    Faber, K.N.2    Wenzel, T.J.3    Koller, A.4    Luers, G.H.5    Rangell, L.6
  • 31
    • 1642394134 scopus 로고    scopus 로고
    • PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins
    • Y. Fang, J.C. Morrell, J.M. Jones, and S.J. Gould PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins J. Cell Biol. 164 2004 775 863
    • (2004) J. Cell Biol. , vol.164 , pp. 775-863
    • Fang, Y.1    Morrell, J.C.2    Jones, J.M.3    Gould, S.J.4
  • 32
    • 0030825248 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Random insertion of a variable five amino acid cassette in a target protein
    • B. Hallet, D.J. Sherratt, and F. Hayes Pentapeptide scanning mutagenesis: random insertion of a variable five amino acid cassette in a target protein Nucl. Acids Res. 25 1997 1866 1867
    • (1997) Nucl. Acids Res. , vol.25 , pp. 1866-1867
    • Hallet, B.1    Sherratt, D.J.2    Hayes, F.3
  • 33
    • 0031588907 scopus 로고    scopus 로고
    • A simple screen for permissive sites in proteins: Analysis of Escherichia coli lac permease
    • C. Manoil, and J. Bailey A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease J. Mol. Biol. 267 1997 250 263
    • (1997) J. Mol. Biol. , vol.267 , pp. 250-263
    • Manoil, C.1    Bailey, J.2
  • 34
    • 4644250692 scopus 로고    scopus 로고
    • Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins
    • H. Shibata, Y. Kashiwayama, T. Imanaka, and H. Kato Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins J. Biol. Chem. 279 2004 38486 38494
    • (2004) J. Biol. Chem. , vol.279 , pp. 38486-38494
    • Shibata, H.1    Kashiwayama, Y.2    Imanaka, T.3    Kato, H.4
  • 35
    • 0033605116 scopus 로고    scopus 로고
    • Recombinant human peroxisomal targeting signal receptor PEX5: Structural basis for interaction of PEX5 with PEX14
    • W. Schliebs, J. Saidowsky, B. Agianian, G. Dodt, F.W. Herberg, and W.H. Kunau Recombinant human peroxisomal targeting signal receptor PEX5: structural basis for interaction of PEX5 with PEX14 J. Biol. Chem. 274 1999 5666 5673
    • (1999) J. Biol. Chem. , vol.274 , pp. 5666-5673
    • Schliebs, W.1    Saidowsky, J.2    Agianian, B.3    Dodt, G.4    Herberg, F.W.5    Kunau, W.H.6
  • 36
    • 0035860787 scopus 로고    scopus 로고
    • The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14
    • J. Saidowsky, G. Dodt, K. Kirchberg, A. Wegner, W. Nastainczyk, W.H. Kunau, and W. Schliebs The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14 J. Biol. Chem. 276 2001 34524 34529
    • (2001) J. Biol. Chem. , vol.276 , pp. 34524-34529
    • Saidowsky, J.1    Dodt, G.2    Kirchberg, K.3    Wegner, A.4    Nastainczyk, W.5    Kunau, W.H.6    Schliebs, W.7
  • 37
    • 0036179374 scopus 로고    scopus 로고
    • Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: Conserved Pex5p WXXXF/Y motifs are critical for matrix protein import
    • H. Otera, K. Setoguchi, M. Hamasaki, T. Kumashiro, N. Shimizu, and Y. Fujiki Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import Mol. Cell. Biol. 22 2002 1639 1655
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1639-1655
    • Otera, H.1    Setoguchi, K.2    Hamasaki, M.3    Kumashiro, T.4    Shimizu, N.5    Fujiki, Y.6
  • 38
    • 0141431060 scopus 로고    scopus 로고
    • Analysis of the sequence motifs responsible for the interactions of peroxins 14 and 5, which are involved in glycosome biogenesis in Trypansoma brucei
    • J. Choe, J. Moyersoen, C. Roach, T.L. Carter, E. Fan, P.A.M. Michels, and W.G.J. Hol Analysis of the sequence motifs responsible for the interactions of peroxins 14 and 5, which are involved in glycosome biogenesis in Trypansoma brucei Biochemistry 42 2003 10915 10922
    • (2003) Biochemistry , vol.42 , pp. 10915-10922
    • Choe, J.1    Moyersoen, J.2    Roach, C.3    Carter, T.L.4    Fan, E.5    Michels, P.A.M.6    Hol, W.G.J.7
  • 40
    • 0037184122 scopus 로고    scopus 로고
    • A major functional difference between the mouse and human ARF tumor suppressor proteins
    • R. Wadhwa, T. Sugihara, M.K. Hasan, K. Taira, R.R. Reddel, and S.C. Kaul A major functional difference between the mouse and human ARF tumor suppressor proteins J. Biol. Chem. 277 2002 36665 36670
    • (2002) J. Biol. Chem. , vol.277 , pp. 36665-36670
    • Wadhwa, R.1    Sugihara, T.2    Hasan, M.K.3    Taira, K.4    Reddel, R.R.5    Kaul, S.C.6
  • 41
    • 1242314750 scopus 로고    scopus 로고
    • Interaction of a farnesylated protein with renal type IIa Na/Pi co-transporter in response to parathyroid hormone and dietary phosphate
    • M. Ito, S. Iidawa, M. Izuka, S. Haito, H. Segawa, and M. Kuwahata Interaction of a farnesylated protein with renal type IIa Na/Pi co-transporter in response to parathyroid hormone and dietary phosphate Biochem. J. 377 2004 607 616
    • (2004) Biochem. J. , vol.377 , pp. 607-616
    • Ito, M.1    Iidawa, S.2    Izuka, M.3    Haito, S.4    Segawa, H.5    Kuwahata, M.6
  • 42
  • 43
    • 0033153285 scopus 로고    scopus 로고
    • Identification of peroxisomal proteins by using M13 phage protein VI phage display: Molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase
    • M. Fransen, P.P. Van Veldhoven, and S. Subramani Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase Biochem. J. 340 1999 561 568
    • (1999) Biochem. J. , vol.340 , pp. 561-568
    • Fransen, M.1    Van Veldhoven, P.P.2    Subramani, S.3
  • 45
    • 0027477526 scopus 로고
    • Structural analysis based on state-space modeling
    • J.M. Stultz, J.V. White, and T.F. Smith Structural analysis based on state-space modeling Protein Sci. 2 1993 305 314
    • (1993) Protein Sci. , vol.2 , pp. 305-314
    • Stultz, J.M.1    White, J.V.2    Smith, T.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.