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Volumn 189, Issue 1, 2010, Pages 11-12

Chaperoning ribosome assembly

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; RIBOSOME PROTEIN; UBIQUITIN;

EID: 77950549733     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201002102     Document Type: Note
Times cited : (12)

References (17)
  • 1
    • 77950573146 scopus 로고    scopus 로고
    • A ribosome-anchored network that facilitates eukaryotic ribosome biogenesis
    • Albanise, V., S. Reissinann, and J. Frydman. 2010. A ribosome-anchored network that facilitates eukaryotic ribosome biogenesis. J. Cell Biol. 189:69-81.
    • (2010) J. Cell Biol. , vol.189 , pp. 69-81
    • Albanise, V.1    Reissinann, S.2    Frydman, J.3
  • 2
    • 0028142992 scopus 로고
    • Protein expression using cotranslational fusion and cleavage of ubiquitin: Mutagenesis of the glutathione-binding site of human Pi class glutathione S-transferase
    • Baker, R. T., S. A. Smith, R. Marano, J. McKee, and P.G. Board. 1994. Protein expression using cotranslational fusion and cleavage of ubiquitin. Mutagenesis of the glutathione-binding site of human Pi class glutathione S-transferase. J. Biol. Chem. 269:25381-25386. (Pubitemid 24982896)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.41 , pp. 25381-25386
    • Baker, R.T.1    Smith, S.A.2    Marano, R.3    McKee, J.4    Board, P.G.5
  • 3
    • 0033642214 scopus 로고    scopus 로고
    • In vitro reconstitution of 30S ribosomal subunits using complete set of recombinant proteins
    • doi: 10.1016/S0076-6879(00)18069-3
    • Culver, G. M., and H. F. Noller. 2000. In vitro reconstitution of 30S ribosomal subunits using complete set of recombinant proteins. Methods Enzymol. 318:446-460. doi: 10.1016/S0076-6879(00)18069-3
    • (2000) Methods Enzymol. , vol.318 , pp. 446-460
    • Culver, G.M.1    Noller, H.F.2
  • 4
    • 34548341809 scopus 로고    scopus 로고
    • The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae
    • DOI 10.1261/rna.585007
    • Demoinet, E., A. Jacquier, G. Lutfalla, and M. Fromont-Racine. 2007. The Hsp40 chaperone Jjjl is required for the nucleo-cytoplasmic recycling of preribosomal factors in Sacchammyces cerevisiae. RNA. 13:1570-1581. doi:10.1261/rna.585007 (Pubitemid 47347427)
    • (2007) RNA , vol.13 , Issue.9 , pp. 1570-1581
    • Demoinet, E.1    Jacquier, A.2    Lutfalla, G.3    Fromont-Racine, M.4
  • 5
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • doi:10.1038/338394a0
    • Finley, D., B. Bartel, and A. Varshavsky. 1989. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature. 338:394-401. doi:10.1038/338394a0
    • (1989) Nature. , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 6
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Sacchammyces cerevisiae: Implications to protein folding pathways in the cell
    • doi:10.1038/msb.2009.26
    • Gong, Y., Y. Kakihara, N. Krogan, J. Greenblatt, A. Emili, Z. Zhang, and W. A. Houry. 2009. An atlas of chaperone-protein interactions in Sacchammyces cerevisiae: implications to protein folding pathways in the cell. Mol. Syst. Biol. 5:275. doi:10.1038/msb.2009.26
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5    Zhang, Z.6    Houry, W.A.7
  • 7
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • doi: 10.1038/ nsmb.1591
    • Hartl, F. U., and M. Hayer-Hartl. 2009. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol Biol. 16:574-581. doi: 10.1038/ nsmb.1591
    • (2009) Nat. Struct. Mol Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 8
    • 77950562866 scopus 로고    scopus 로고
    • A dual function for chaperones Ssb-RAC and the NAC nascent polypeptide-associated complex on ribosomes
    • Koplin, A., S. Preisler, Y. Ilina, M. Koch, A. Scior, M. Erhardt, and E. Deuerling. 2010. A dual function for chaperones Ssb-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J. Cell Biol. 189:57-68.
    • (2010) J. Cell Biol. , vol.189 , pp. 57-68
    • Koplin, A.1    Preisler, S.2    Ilina, Y.3    Koch, M.4    Scior, A.5    Erhardt, M.6    Deuerling, E.7
  • 9
    • 62949242460 scopus 로고    scopus 로고
    • Linear ubiquitin fusion to Rps31 and its subsequent cleavage are required for the efficient production and functional integrity of 40S ribosomal subunits
    • doi:10.1111/j.13652958.2009.06622.x
    • Lacombe, T., J. J. García-Gómez, J. de la Cruz, D. Roser, E. Hurt, P. Linder, and D. Kressler. 2009. Linear ubiquitin fusion to Rps31 and its subsequent cleavage are required for the efficient production and functional integrity of 40S ribosomal subunits. Mol. Microbiol. 72:69-84. doi:10.1111/j.13652958.2009.06622.x
    • (2009) Mol. Microbiol. , vol.72 , pp. 69-84
    • Lacombe, T.1    García-Gómez, J.J.2    De La Cruz, J.3    Roser, D.4    Hurt, E.5    Linder, P.6    Kressler, D.7
  • 10
    • 70149120737 scopus 로고    scopus 로고
    • Nob1 binds the single-stranded cleavage site D at the 3'-end of 18S rRNA with its PIN domain
    • doi:10.1073/pnas.0905403106
    • Lamanna, A. C., and K. Karbstein. 2009. Nob1 binds the single-stranded cleavage site D at the 3'-end of 18S rRNA with its PIN domain. Proc. Natl. Acad. Sci. USA. 106:14259-14264. doi:10.1073/pnas.0905403106
    • (2009) Proc. Natl. Acad. Sci. USA. , vol.106 , pp. 14259-14264
    • Lamanna, A.C.1    Karbstein, K.2
  • 11
    • 0036342369 scopus 로고    scopus 로고
    • The DnaK chaperone system facilitates 30S ribosomal subunit assembly
    • doi:10.1016/S1097-2765(02)00562-2
    • Maki, J. A., D. J. Schnobrich, and G. M. Culver. 2002. The DnaK chaperone system facilitates 30S ribosomal subunit assembly. Mol. Cell. 10:129-138. doi:10.1016/S1097-2765(02)00562-2
    • (2002) Mol. Cell. , vol.10 , pp. 129-138
    • Maki, J.A.1    Schnobrich, D.J.2    Culver, G.M.3
  • 12
    • 69449095153 scopus 로고    scopus 로고
    • Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone
    • doi:10.1016/j.cell.2009.07.044
    • Martinez-Hackert, E., and W. A. Hendrickson. 2009. Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell. 138:923-934. doi:10.1016/j.cell.2009.07.044
    • (2009) Cell. , vol.138 , pp. 923-934
    • Martinez-Hackert, E.1    Hendrickson, W.A.2
  • 13
    • 33846818906 scopus 로고    scopus 로고
    • The specialized cytosolic J-protein, Jjj 1, functions in 60S ribosomal subunit biogenesis
    • do:i:10.1073/ pnas.0610704104
    • Meyer, A. E., N. J. Hung, P. Yang, A. W. Johnson, and E. A. Craig. 2007. The specialized cytosolic J-protein, Jjj 1, functions in 60S ribosomal subunit biogenesis. Proc. Natl. Acad. Sci. USA. 104:1558-1563. do:i:10.1073/ pnas.0610704104
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 1558-1563
    • Meyer, A.E.1    Hung, N.J.2    Yang, P.3    Johnson, A.W.4    Craig, E.A.5
  • 14
    • 74049138306 scopus 로고    scopus 로고
    • The cytosolic J-protein, Jjj1, and Reil function in the removal of the pre-60 S subunit factor Arxl
    • doi:10.1074/jbc.M109.038349
    • Meyer, A. E., L. A. Hoover, and E. A. Craig. 2010. The cytosolic J-protein, Jjj1, and Reil function in the removal of the pre-60 S subunit factor Arxl. J. Biol. Chem. 285:961-968. doi:10.1074/jbc.M109.038349
    • (2010) J. Biol. Chem. , vol.285 , pp. 961-968
    • Meyer, A.E.1    Hoover, L.A.2    Craig, E.A.3
  • 15
    • 73249132431 scopus 로고    scopus 로고
    • Powering through ribosome assembly
    • doi:10.1261/rna.1792109
    • Strunk, B. S., and K. Karbstein. 2009. Powering through ribosome assembly. RNA. 15:2083-2104. doi:10.1261/rna.1792109
    • (2009) RNA. , vol.15 , pp. 2083-2104
    • Strunk, B.S.1    Karbstein, K.2
  • 16
    • 0014693477 scopus 로고
    • Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30 s ribosomes studied in vitro
    • doi: 10.1016/0022-2836(69)90161 -2
    • Traub, P., and M. Nomura. 1969. Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30 s ribosomes studied in vitro. J. Mol. Biol. 40:391-413. doi: 10.1016/0022-2836(69)90161 -2
    • (1969) J. Mol. Biol. , vol.40 , pp. 391-413
    • Traub, P.1    Nomura, M.2
  • 17
    • 0032541489 scopus 로고    scopus 로고
    • Zuotin, a ribosome-associated DnaJ molecular chaperone
    • doi:10.1093/emboj/17.16.4809
    • Yan, W., B. Schilke, C. Pfund, W. Walter, S. Kim, and E. A. Craig. 1998. Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17:48094817. doi:10.1093/emboj/17.16.4809
    • (1998) EMBO J. , vol.17 , pp. 48094817
    • Yan, W.1    Schilke, B.2    Pfund, C.3    Walter, W.4    Kim, S.5    Craig, E.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.