메뉴 건너뛰기




Volumn 8, Issue 1, 2014, Pages 59-65

Cryoelectron microscopic structures of eukaryotic translation termination complexes containing eRF1-eRF3 or eRF1-ABCE1

Author keywords

[No Author keywords available]

Indexed keywords

ABC ENZYME 1; EUKARYOTIC RELEASE FACTOR 1; EUKARYOTIC RELEASE FACTOR 2; EUKARYOTIC RELEASE FACTOR 3; MEMBRANE PROTEIN; PEPTIDYLTRANSFERASE; UNCLASSIFIED DRUG; ABC TRANSPORTER; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSLATION TERMINATION FACTOR; VEGETABLE PROTEIN; FUNGAL PROTEIN; PROTEIN ABCE1; PROTEIN ERF1; PROTEIN ERF3;

EID: 84904434651     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2014.04.058     Document Type: Article
Times cited : (89)

References (28)
  • 1
    • 33744993160 scopus 로고    scopus 로고
    • Invitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3
    • Alkalaeva E.Z., Pisarev A.V., Frolova L.Y., Kisselev L.L., Pestova T.V. Invitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 2006, 125:1125-1136.
    • (2006) Cell , vol.125 , pp. 1125-1136
    • Alkalaeva, E.Z.1    Pisarev, A.V.2    Frolova, L.Y.3    Kisselev, L.L.4    Pestova, T.V.5
  • 2
    • 79952750280 scopus 로고    scopus 로고
    • Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1
    • Barthelme D., Dinkelaker S., Albers S.V., Londei P., Ermler U., Tampé R. Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1. Proc. Natl. Acad. Sci. USA 2011, 108:3228-3233.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3228-3233
    • Barthelme, D.1    Dinkelaker, S.2    Albers, S.V.3    Londei, P.4    Ermler, U.5    Tampé, R.6
  • 8
    • 33645277360 scopus 로고    scopus 로고
    • Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation
    • Doma M.K., Parker R. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 2006, 440:561-564.
    • (2006) Nature , vol.440 , pp. 561-564
    • Doma, M.K.1    Parker, R.2
  • 9
    • 84870391243 scopus 로고    scopus 로고
    • Structural view on recycling of archaeal and eukaryotic ribosomes after canonical termination and ribosome rescue
    • Franckenberg S., Becker T., Beckmann R. Structural view on recycling of archaeal and eukaryotic ribosomes after canonical termination and ribosome rescue. Curr. Opin. Struct. Biol. 2012, 22:786-796.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 786-796
    • Franckenberg, S.1    Becker, T.2    Beckmann, R.3
  • 10
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J.Struct. Biol. 1996, 116:190-199.
    • (1996) J.Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 11
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
    • Freistroffer D.V., Pavlov M.Y., MacDougall J., Buckingham R.H., Ehrenberg M. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J. 1997, 16:4126-4133.
    • (1997) EMBO J. , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 12
    • 19244364778 scopus 로고    scopus 로고
    • Eukaryotic polypeptide chain release factor eRF3 is aneRF1- and ribosome-dependent guanosine triphosphatase
    • Frolova L., Le Goff X., Zhouravleva G., Davydova E., Philippe M., Kisselev L. Eukaryotic polypeptide chain release factor eRF3 is aneRF1- and ribosome-dependent guanosine triphosphatase. RNA 1996, 2:334-341.
    • (1996) RNA , vol.2 , pp. 334-341
    • Frolova, L.1    Le Goff, X.2    Zhouravleva, G.3    Davydova, E.4    Philippe, M.5    Kisselev, L.6
  • 14
    • 0036893271 scopus 로고    scopus 로고
    • Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA
    • Janzen D.M., Frolova L., Geballe A.P. Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA. Mol. Cell. Biol. 2002, 22:8562-8570.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8562-8570
    • Janzen, D.M.1    Frolova, L.2    Geballe, A.P.3
  • 16
    • 43149119755 scopus 로고    scopus 로고
    • X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi
    • Karcher A., Schele A., Hopfner K.P. X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi. J.Biol. Chem. 2008, 283:7962-7971.
    • (2008) J.Biol. Chem. , vol.283 , pp. 7962-7971
    • Karcher, A.1    Schele, A.2    Hopfner, K.P.3
  • 17
    • 1942470550 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe
    • Kong C., Ito K., Walsh M.A., Wada M., Liu Y., Kumar S., Barford D., Nakamura Y., Song H. Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Mol. Cell 2004, 14:233-245.
    • (2004) Mol. Cell , vol.14 , pp. 233-245
    • Kong, C.1    Ito, K.2    Walsh, M.A.3    Wada, M.4    Liu, Y.5    Kumar, S.6    Barford, D.7    Nakamura, Y.8    Song, H.9
  • 23
    • 79955626576 scopus 로고    scopus 로고
    • Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
    • Pisareva V.P., Skabkin M.A., Hellen C.U., Pestova T.V., Pisarev A.V. Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes. EMBO J. 2011, 30:1804-1817.
    • (2011) EMBO J. , vol.30 , pp. 1804-1817
    • Pisareva, V.P.1    Skabkin, M.A.2    Hellen, C.U.3    Pestova, T.V.4    Pisarev, A.V.5
  • 24
    • 84855501083 scopus 로고    scopus 로고
    • Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast
    • Shoemaker C.J., Green R. Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc. Natl. Acad. Sci. USA 2011, 108:E1392-E1398.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108
    • Shoemaker, C.J.1    Green, R.2
  • 25
    • 77957935294 scopus 로고    scopus 로고
    • Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay
    • Shoemaker C.J., Eyler D.E., Green R. Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 2010, 330:369-372.
    • (2010) Science , vol.330 , pp. 369-372
    • Shoemaker, C.J.1    Eyler, D.E.2    Green, R.3
  • 26
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song H., Mugnier P., Das A.K., Webb H.M., Evans D.R., Tuite M.F., Hemmings B.A., Barford D. The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 2000, 100:311-321.
    • (2000) Cell , vol.100 , pp. 311-321
    • Song, H.1    Mugnier, P.2    Das, A.K.3    Webb, H.M.4    Evans, D.R.5    Tuite, M.F.6    Hemmings, B.A.7    Barford, D.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.