메뉴 건너뛰기




Volumn 7, Issue 10, 2012, Pages

Split-Doa10: A Naturally Split Polytopic Eukaryotic Membrane Protein Generated by Fission of a Nuclear Gene

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; SPLIT DOA10 PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84867116845     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0045194     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 2342578691 scopus 로고    scopus 로고
    • Internal gene duplication in the evolution of prokaryotic transmembrane proteins
    • Shimizu T, Mitsuke H, Noto K, Arai M, (2004) Internal gene duplication in the evolution of prokaryotic transmembrane proteins. J Mol Biol 339: 1-15.
    • (2004) J Mol Biol , vol.339 , pp. 1-15
    • Shimizu, T.1    Mitsuke, H.2    Noto, K.3    Arai, M.4
  • 2
    • 0030309453 scopus 로고    scopus 로고
    • Phylogenetic approaches to the identification and characterization of protein families and superfamilies
    • Saier MH Jr, (1996) Phylogenetic approaches to the identification and characterization of protein families and superfamilies. Microb Comp Genomics 1: 129-150.
    • (1996) Microb Comp Genomics , vol.1 , pp. 129-150
    • Saier Jr., M.H.1
  • 3
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, et al. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301: 610-615.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5
  • 4
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot JL, Engelman DM, (2000) Helical membrane protein folding, stability, and evolution. Annu Rev Biochem 69: 881-922.
    • (2000) Annu Rev Biochem , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 5
    • 0017078727 scopus 로고
    • Restoration of calcium transport in the trypsin-treated (Ca+ + Mg2+)-dependent adenosine triphosphatase of sarcoplasmic reticulum exposed th sodium dodecyl sulfate
    • MacLennan DH, Khanna VK, Stewart PS, (1976) Restoration of calcium transport in the trypsin-treated (Ca+ + Mg2+)-dependent adenosine triphosphatase of sarcoplasmic reticulum exposed th sodium dodecyl sulfate. J Biol Chem 251: 7271-7274.
    • (1976) J Biol Chem , vol.251 , pp. 7271-7274
    • MacLennan, D.H.1    Khanna, V.K.2    Stewart, P.S.3
  • 6
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang KS, Bayley H, Liao MJ, London E, Khorana HG, (1981) Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J Biol Chem 256: 3802-3809.
    • (1981) J Biol Chem , vol.256 , pp. 3802-3809
    • Huang, K.S.1    Bayley, H.2    Liao, M.J.3    London, E.4    Khorana, H.G.5
  • 7
    • 0021338738 scopus 로고
    • Regeneration of native bacteriorhodopsin structure from fragments
    • Liao MJ, Huang KS, Khorana HG, (1984) Regeneration of native bacteriorhodopsin structure from fragments. J Biol Chem 259: 4200-4204.
    • (1984) J Biol Chem , vol.259 , pp. 4200-4204
    • Liao, M.J.1    Huang, K.S.2    Khorana, H.G.3
  • 8
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of alpha-helical integral membrane proteins
    • Mackenzie KR, (2006) Folding and stability of alpha-helical integral membrane proteins. Chem Rev 106: 1931-1977.
    • (2006) Chem Rev , vol.106 , pp. 1931-1977
    • Mackenzie, K.R.1
  • 9
    • 0034913239 scopus 로고    scopus 로고
    • The origin and early evolution of mitochondria
    • Gray MW, Burger G, Lang BF, (2001) The origin and early evolution of mitochondria. Genome Biol 2: REVIEWS1018.
    • (2001) Genome Biol , vol.2
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 10
    • 0344719444 scopus 로고    scopus 로고
    • Evolution of mitochondrial gene content: gene loss and transfer to the nucleus
    • Adams KL, Palmer JD, (2003) Evolution of mitochondrial gene content: gene loss and transfer to the nucleus. Mol Phylogenet Evol 29: 380-395.
    • (2003) Mol Phylogenet Evol , vol.29 , pp. 380-395
    • Adams, K.L.1    Palmer, J.D.2
  • 11
    • 72649086890 scopus 로고    scopus 로고
    • An ancient fission of mitochondrial Cox1
    • Gawryluk RM, Gray MW, (2010) An ancient fission of mitochondrial Cox1. Mol Biol Evol 27: 7-10.
    • (2010) Mol Biol Evol , vol.27 , pp. 7-10
    • Gawryluk, R.M.1    Gray, M.W.2
  • 12
    • 0346041565 scopus 로고    scopus 로고
    • Subunit II of cytochrome c oxidase in Chlamydomonad algae is a heterodimer encoded by two independent nuclear genes
    • Perez-Martinez X, Antaramian A, Vazquez-Acevedo M, Funes S, Tolkunova E, et al. (2001) Subunit II of cytochrome c oxidase in Chlamydomonad algae is a heterodimer encoded by two independent nuclear genes. J Biol Chem 276: 11302-11309.
    • (2001) J Biol Chem , vol.276 , pp. 11302-11309
    • Perez-Martinez, X.1    Antaramian, A.2    Vazquez-Acevedo, M.3    Funes, S.4    Tolkunova, E.5
  • 13
    • 54449100867 scopus 로고    scopus 로고
    • The three mitochondrial encoded CcmF proteins form a complex that interacts with CCMH and c-type apocytochromes in Arabidopsis
    • Rayapuram N, Hagenmuller J, Grienenberger JM, Bonnard G, Giege P, (2008) The three mitochondrial encoded CcmF proteins form a complex that interacts with CCMH and c-type apocytochromes in Arabidopsis. J Biol Chem 283: 25200-25208.
    • (2008) J Biol Chem , vol.283 , pp. 25200-25208
    • Rayapuram, N.1    Hagenmuller, J.2    Grienenberger, J.M.3    Bonnard, G.4    Giege, P.5
  • 14
    • 55449129926 scopus 로고    scopus 로고
    • Fusion and fission of genes define a metric between fungal genomes
    • Durrens P, Nikolski M, Sherman D, (2008) Fusion and fission of genes define a metric between fungal genomes. PLoS Comput Biol 4: e1000200.
    • (2008) PLoS Comput Biol , vol.4
    • Durrens, P.1    Nikolski, M.2    Sherman, D.3
  • 15
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson R, Locher M, Hochstrasser M, (2001) A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev 15: 2660-2674.
    • (2001) Genes Dev , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 16
    • 33646185061 scopus 로고    scopus 로고
    • Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)
    • Kreft SG, Wang L, Hochstrasser M, (2006) Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J Biol Chem 281: 4646-4653.
    • (2006) J Biol Chem , vol.281 , pp. 4646-4653
    • Kreft, S.G.1    Wang, L.2    Hochstrasser, M.3
  • 17
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng M, Hochstrasser M, (2006) Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature 443: 827-831.
    • (2006) Nature , vol.443 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 18
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • Ravid T, Kreft SG, Hochstrasser M, (2006) Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J 25: 533-543.
    • (2006) EMBO J , vol.25 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 19
    • 79958015229 scopus 로고    scopus 로고
    • An unusual transmembrane helix in the Doa10 ERAD ubiquitin ligase modulates degradation of its cognate E2
    • Kreft SG, Hochstrasser M, (2011) An unusual transmembrane helix in the Doa10 ERAD ubiquitin ligase modulates degradation of its cognate E2. J Biol Chem.
    • (2011) J Biol Chem
    • Kreft, S.G.1    Hochstrasser, M.2
  • 20
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor
    • Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M, (1993) Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. Cell 74: 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 21
    • 0030845189 scopus 로고    scopus 로고
    • VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H+-ATPase assembly
    • Jackson DD, Stevens TH, (1997) VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H+-ATPase assembly. J Biol Chem 272: 25928-25934.
    • (1997) J Biol Chem , vol.272 , pp. 25928-25934
    • Jackson, D.D.1    Stevens, T.H.2
  • 22
    • 0344256533 scopus 로고    scopus 로고
    • Phylogenetic circumscription of Saccharomyces, Kluyveromyces and other members of the Saccharomycetaceae, and the proposal of the new genera Lachancea, Nakaseomyces, Naumovia, Vanderwaltozyma and Zygotorulaspora
    • Kurtzman CP, (2003) Phylogenetic circumscription of Saccharomyces, Kluyveromyces and other members of the Saccharomycetaceae, and the proposal of the new genera Lachancea, Nakaseomyces, Naumovia, Vanderwaltozyma and Zygotorulaspora. FEMS Yeast Res 4: 233-245.
    • (2003) FEMS Yeast Res , vol.4 , pp. 233-245
    • Kurtzman, C.P.1
  • 23
    • 34447298401 scopus 로고    scopus 로고
    • Current status of Kluyveromyces systematics
    • Lachance MA, (2007) Current status of Kluyveromyces systematics. FEMS Yeast Res 7: 642-645.
    • (2007) FEMS Yeast Res , vol.7 , pp. 642-645
    • Lachance, M.A.1
  • 25
    • 0034704335 scopus 로고    scopus 로고
    • Genomic exploration of the hemiascomycetous yeasts: 12. Kluyveromyces marxianus var. marxianus
    • Llorente B, Malpertuy A, Blandin G, Artiguenave F, Wincker P, et al. (2000) Genomic exploration of the hemiascomycetous yeasts: 12. Kluyveromyces marxianus var. marxianus. FEBS Lett 487: 71-75.
    • (2000) FEBS Lett , vol.487 , pp. 71-75
    • Llorente, B.1    Malpertuy, A.2    Blandin, G.3    Artiguenave, F.4    Wincker, P.5
  • 26
    • 79956293316 scopus 로고    scopus 로고
    • Extensive DNA-binding specificity divergence of a conserved transcription regulator
    • Baker CR, Tuch BB, Johnson AD, (2011) Extensive DNA-binding specificity divergence of a conserved transcription regulator. Proc Natl Acad Sci U S A 108: 7493-7498.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 7493-7498
    • Baker, C.R.1    Tuch, B.B.2    Johnson, A.D.3
  • 27
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins
    • Bartee E, Mansouri M, Hovey Nerenberg BT, Gouveia K, Fruh K, (2004) Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J Virol 78: 1109-1120.
    • (2004) J Virol , vol.78 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Hovey Nerenberg, B.T.3    Gouveia, K.4    Fruh, K.5
  • 28
    • 67349172917 scopus 로고    scopus 로고
    • The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases
    • Nathan JA, Lehner PJ, (2009) The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases. Exp Cell Res 315: 1593-1600.
    • (2009) Exp Cell Res , vol.315 , pp. 1593-1600
    • Nathan, J.A.1    Lehner, P.J.2
  • 29
    • 56949087771 scopus 로고    scopus 로고
    • Viral and cellular MARCH ubiquitin ligases and cancer
    • Wang X, Herr RA, Hansen T, (2008) Viral and cellular MARCH ubiquitin ligases and cancer. Semin Cancer Biol 18: 441-450.
    • (2008) Semin Cancer Biol , vol.18 , pp. 441-450
    • Wang, X.1    Herr, R.A.2    Hansen, T.3
  • 30
    • 79955598535 scopus 로고    scopus 로고
    • Insights into the evolution of Archaea and eukaryotic protein modifier systems revealed by the genome of a novel archaeal group
    • Nunoura T, Takaki Y, Kakuta J, Nishi S, Sugahara J, et al. (2011) Insights into the evolution of Archaea and eukaryotic protein modifier systems revealed by the genome of a novel archaeal group. Nucleic Acids Res 39: 3204-3223.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3204-3223
    • Nunoura, T.1    Takaki, Y.2    Kakuta, J.3    Nishi, S.4    Sugahara, J.5
  • 31
    • 79959214387 scopus 로고    scopus 로고
    • Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system
    • Burroughs AM, Iyer LM, Aravind L, (2011) Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system. Mol Biosyst 7: 2261-2277.
    • (2011) Mol Biosyst , vol.7 , pp. 2261-2277
    • Burroughs, A.M.1    Iyer, L.M.2    Aravind, L.3
  • 33
  • 34
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt ME, Brown TA, Trumpower BL, (1990) A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res 18: 3091-3092.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.