메뉴 건너뛰기




Volumn 22, Issue 24, 2003, Pages 6562-6572

A La protein requirement for efficient pre-tRNA folding

Author keywords

Aminoacylation; La autoantigen; Pre tRNA folding

Indexed keywords

EXONUCLEASE; LA ANTIGEN; LHP1P PROTEIN; RNA PRECURSOR; TRANSFER RNA; TRANSFER RNA PRECURSOR; UNCLASSIFIED DRUG;

EID: 0347747969     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg625     Document Type: Article
Times cited : (101)

References (41)
  • 1
    • 0032428969 scopus 로고    scopus 로고
    • The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA
    • Anderson, J., Phan, L., Cuesta, R., Carlson, B.A., Pak, M., Asano, K., Bjork, G.R., Tamame, M. and Hinnebusch, A.G. (1998) The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev., 12, 3650-3662.
    • (1998) Genes Dev. , vol.12 , pp. 3650-3662
    • Anderson, J.1    Phan, L.2    Cuesta, R.3    Carlson, B.A.4    Pak, M.5    Asano, K.6    Bjork, G.R.7    Tamame, M.8    Hinnebusch, A.G.9
  • 2
    • 0024356434 scopus 로고
    • U5 small nuclear ribonucleoprotein: RNA structure analysis and ATP-dependent interaction with U4/U6
    • Black, D.L. and Pinto, A.L. (1989) U5 small nuclear ribonucleoprotein: RNA structure analysis and ATP-dependent interaction with U4/U6. Mol. Cell. Biol., 9, 3350-3359.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3350-3359
    • Black, D.L.1    Pinto, A.L.2
  • 3
    • 0033169013 scopus 로고    scopus 로고
    • Assaying RNA chaperone activity in vivo using a novel RNA folding trap
    • Clodi, E., Semrad, K. and Schroeder, R. (1999) Assaying RNA chaperone activity in vivo using a novel RNA folding trap. EMBO J., 18, 3776-3782.
    • (1999) EMBO J. , vol.18 , pp. 3776-3782
    • Clodi, E.1    Semrad, K.2    Schroeder, R.3
  • 4
    • 0027273672 scopus 로고
    • A cold-sensitive mutation in 16S rRNA provides evidence for helical switching in ribosome assembly
    • Dammel, C.S. and Noller, H.F. (1993) A cold-sensitive mutation in 16S rRNA provides evidence for helical switching in ribosome assembly. Genes Dev., 7, 660-670.
    • (1993) Genes Dev. , vol.7 , pp. 660-670
    • Dammel, C.S.1    Noller, H.F.2
  • 5
    • 0034332436 scopus 로고    scopus 로고
    • tRNA aminoacylation by arginyl-tRNA synthetase: Induced conformations during substrates binding
    • Delagoutte, B., Moras, D. and Cavarelli, J. (2000) tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding. EMBO J., 19, 5599-5610.
    • (2000) EMBO J. , vol.19 , pp. 5599-5610
    • Delagoutte, B.1    Moras, D.2    Cavarelli, J.3
  • 6
    • 0027935988 scopus 로고
    • Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trm1 tRNA-modifying enzyme
    • Edqvist, J., Blomqvist, K. and Straby, K.B. (1994) Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trm1 tRNA-modifying enzyme. Biochemistry, 33, 9546-9551.
    • (1994) Biochemistry , vol.33 , pp. 9546-9551
    • Edqvist, J.1    Blomqvist, K.2    Straby, K.B.3
  • 7
    • 0036848963 scopus 로고    scopus 로고
    • The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a putative DEAH-box RNA helicase
    • Fouraux, M.A., Kolkman, M.J., Van der Heijden, A., De Jong, A.S., Van Venrooij, W.J. and Pruijn, G.J. (2002) The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a putative DEAH-box RNA helicase. RNA, 8, 1428-1443.
    • (2002) RNA , vol.8 , pp. 1428-1443
    • Fouraux, M.A.1    Kolkman, M.J.2    Van Der Heijden, A.3    De Jong, A.S.4    Van Venrooij, W.J.5    Pruijn, G.J.6
  • 8
    • 0013901577 scopus 로고
    • Two interconvertible forms of tryptophanyl sRNA in E. coli
    • Gartland, W.J. and Sueoka, N. (1966) Two interconvertible forms of tryptophanyl sRNA in E. coli. Proc. Natl Acad. Sci. USA, 55, 948-956.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 948-956
    • Gartland, W.J.1    Sueoka, N.2
  • 10
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag, D. (1995) RNA chaperones and the RNA folding problem. J. Biol. Chem., 270, 20871-20874.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 11
    • 0037439213 scopus 로고    scopus 로고
    • tRNA transfers to the limelight
    • Hopper, A.K. and Phizicky, E.M. (2003) tRNA transfers to the limelight. Genes Dev., 17, 162-180.
    • (2003) Genes Dev. , vol.17 , pp. 162-180
    • Hopper, A.K.1    Phizicky, E.M.2
  • 13
    • 0036226647 scopus 로고    scopus 로고
    • Dual function of the tRNA(m(5)U54)methyltransferase in tRNA maturation
    • Johansson, M.J. and Bystrom, A.S. (2002) Dual function of the tRNA(m(5)U54)methyltransferase in tRNA maturation. RNA, 8, 324-335.
    • (2002) RNA , vol.8 , pp. 324-335
    • Johansson, M.J.1    Bystrom, A.S.2
  • 14
    • 0035815744 scopus 로고    scopus 로고
    • Fragile T-stem in disease-associated human mitochondrial tRNA sensitizes structure to local and distant mutations
    • Kelley, S.O., Steinberg, S.V. and Schimmel, P. (2001) Fragile T-stem in disease-associated human mitochondrial tRNA sensitizes structure to local and distant mutations. J. Biol. Chem., 276, 10607-10611.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10607-10611
    • Kelley, S.O.1    Steinberg, S.V.2    Schimmel, P.3
  • 15
    • 0024828055 scopus 로고
    • A guide for probing native small nuclear RNA and ribonucleoprotein structures
    • Krol, A. and Carbon, P. (1989) A guide for probing native small nuclear RNA and ribonucleoprotein structures. Methods Enzymol., 180, 212-227.
    • (1989) Methods Enzymol. , vol.180 , pp. 212-227
    • Krol, A.1    Carbon, P.2
  • 16
    • 0033912221 scopus 로고    scopus 로고
    • Precursors to the U3 small nucleolar RNA lack small nucleolar RNP proteins but are stabilized by La binding
    • Kufel, J., Allmang, C., Chanfreau, G., Petfalski, E., Lafontaine, D.L. and Tollervey, D. (2000) Precursors to the U3 small nucleolar RNA lack small nucleolar RNP proteins but are stabilized by La binding. Mol. Cell. Biol., 20, 5415-5424.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5415-5424
    • Kufel, J.1    Allmang, C.2    Chanfreau, G.3    Petfalski, E.4    Lafontaine, D.L.5    Tollervey, D.6
  • 18
    • 0013898917 scopus 로고
    • Renaturation of transfer ribonucleic acids through site binding of magnesium
    • Lindahl, T., Adams, A. and Fresco, J.R. (1966) Renaturation of transfer ribonucleic acids through site binding of magnesium. Proc. Natl Acad. Sci. USA, 55, 941-948.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 941-948
    • Lindahl, T.1    Adams, A.2    Fresco, J.R.3
  • 19
    • 0035163788 scopus 로고    scopus 로고
    • Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization
    • Long, K.S., Cedervall, T., Walch-Solimena, C., Noe, D.A., Huddleston, M.J., Annan, R.S. and Wolin, S.L. (2001) Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization. RNA, 7, 1589-1602.
    • (2001) RNA , vol.7 , pp. 1589-1602
    • Long, K.S.1    Cedervall, T.2    Walch-Solimena, C.3    Noe, D.A.4    Huddleston, M.J.5    Annan, R.S.6    Wolin, S.L.7
  • 20
    • 0022973884 scopus 로고
    • On the recognition of helical RNA by cobra venom VI nuclease
    • Lowman, H.B. and Draper, D.E. (1986) On the recognition of helical RNA by cobra venom VI nuclease. J. Biol. Chem., 261, 5396-5403.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5396-5403
    • Lowman, H.B.1    Draper, D.E.2
  • 21
    • 0002382573 scopus 로고    scopus 로고
    • The genomic tag hypothesis: What molecular fossils tell us about the evolution of tRNA
    • Gesteland, R., Cech, T.R. and Atkins, J.F. (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Maizels, N. and Weiner, A.M. (1999) The genomic tag hypothesis: what molecular fossils tell us about the evolution of tRNA. In Gesteland, R., Cech, T.R. and Atkins, J.F. (eds), The RNA World. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 79-111.
    • (1999) The RNA World , pp. 79-111
    • Maizels, N.1    Weiner, A.M.2
  • 22
    • 0037077127 scopus 로고    scopus 로고
    • A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • Mohr, S., Stryker, J.M. and Lambowitz, A.M. (2002) A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell, 109, 769-779.
    • (2002) Cell , vol.109 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 23
    • 0037367939 scopus 로고    scopus 로고
    • RNA chaperone activity of the Sm-like Hfq protein
    • Moll, I., Leitsch, D., Steinhauser, T. and Blasi, U. (2003) RNA chaperone activity of the Sm-like Hfq protein. EMBO Rep., 4, 284-289.
    • (2003) EMBO Rep. , vol.4 , pp. 284-289
    • Moll, I.1    Leitsch, D.2    Steinhauser, T.3    Blasi, U.4
  • 24
    • 0032535451 scopus 로고    scopus 로고
    • A role for the yeast La protein in U6 snRNP assembly: Evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts
    • Pannone, B.K., Xue, D. and Wolin, S.L. (1998) A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts. EMBO J., 17, 7442-7453.
    • (1998) EMBO J. , vol.17 , pp. 7442-7453
    • Pannone, B.K.1    Xue, D.2    Wolin, S.L.3
  • 25
    • 0035022015 scopus 로고    scopus 로고
    • Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA and the yeast La protein
    • Pannone, B.K., Kim, S.D., Noe, D.A. and Wolin, S.L. (2001) Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA and the yeast La protein. Genetics, 158, 187-196.
    • (2001) Genetics , vol.158 , pp. 187-196
    • Pannone, B.K.1    Kim, S.D.2    Noe, D.A.3    Wolin, S.L.4
  • 26
    • 0019961077 scopus 로고
    • Precursor molecules of both human 5S ribosomal RNA and transfer RNAs are bound by a cellular protein reactive with anti-La lupus antibodies
    • Rinke, J. and Steitz, J.A. (1982) Precursor molecules of both human 5S ribosomal RNA and transfer RNAs are bound by a cellular protein reactive with anti-La lupus antibodies. Cell, 29, 149-159.
    • (1982) Cell , vol.29 , pp. 149-159
    • Rinke, J.1    Steitz, J.A.2
  • 28
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods Enzymol., 194, 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 29
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 30
    • 0029842244 scopus 로고    scopus 로고
    • Arginine aminoacylation identify is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts
    • Sissler, M., Giege, R. and Florentz, C. (1996) Arginine aminoacylation identify is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts. EMBO J., 15, 5069-5076.
    • (1996) EMBO J. , vol.15 , pp. 5069-5076
    • Sissler, M.1    Giege, R.2    Florentz, C.3
  • 31
    • 0029400768 scopus 로고
    • A correlation between N2-dimethylguanosine presence and alternate tRNA conformers
    • Steinberg, S. and Cedergren, R. (1995) A correlation between N2-dimethylguanosine presence and alternate tRNA conformers. RNA, 1, 886-891.
    • (1995) RNA , vol.1 , pp. 886-891
    • Steinberg, S.1    Cedergren, R.2
  • 32
    • 0028034999 scopus 로고
    • La autoantigen alleviates translational repression by the 5′ leader sequence of the human immunodeficiency virus type 1 mRNA
    • Svitkin, Y.V., Pause, A. and Sonenberg, N. (1994) La autoantigen alleviates translational repression by the 5′ leader sequence of the human immunodeficiency virus type 1 mRNA. J. Virol., 68, 7001-7007.
    • (1994) J. Virol. , vol.68 , pp. 7001-7007
    • Svitkin, Y.V.1    Pause, A.2    Sonenberg, N.3
  • 33
    • 0029258928 scopus 로고
    • Keeping RNA happy
    • Uhlenbeck, O.C. (1995) Keeping RNA happy. RNA, 1, 4-6.
    • (1995) RNA , vol.1 , pp. 4-6
    • Uhlenbeck, O.C.1
  • 34
    • 0031469506 scopus 로고    scopus 로고
    • The La protein in Schizosaccharomyces pombe: A conserved yet dispensable phosphoprotein that functions in tRNA maturation
    • Van Horn, D.J., Yoo, C.J., Xue, D., Shi, H. and Wolin, S.L. (1997) The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation. RNA, 3, 1434-1443.
    • (1997) RNA , vol.3 , pp. 1434-1443
    • Van Horn, D.J.1    Yoo, C.J.2    Xue, D.3    Shi, H.4    Wolin, S.L.5
  • 35
    • 0026350896 scopus 로고
    • Direct analysis of aminoacylation levels of tRNAs in vivo. Application to studying recognition of Escherichia coli initiator tRNA mutants by glutaminyl-tRNA synthetase
    • Varshney, U., Lee, C.P. and RajBhandary, U.L. (1991) Direct analysis of aminoacylation levels of tRNAs in vivo. Application to studying recognition of Escherichia coli initiator tRNA mutants by glutaminyl-tRNA synthetase. J. Biol. Chem., 266, 24712-24718.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24712-24718
    • Varshney, U.1    Lee, C.P.2    RajBhandary, U.L.3
  • 37
    • 0034599747 scopus 로고    scopus 로고
    • U snRNP assembly in yeast involves the La protein
    • Xue, D., Rubinson, D.A., Pannone, B.K., Yoo, C.J. and Wolin, S.L. (2000) U snRNP assembly in yeast involves the La protein. EMBO J., 19, 1650-1660.
    • (2000) EMBO J. , vol.19 , pp. 1650-1660
    • Xue, D.1    Rubinson, D.A.2    Pannone, B.K.3    Yoo, C.J.4    Wolin, S.L.5
  • 38
    • 0030904723 scopus 로고    scopus 로고
    • The yeast La protein is required for the 3′ endonucleolytic cleavage that matures tRNA precursors
    • Yoo, C.J. and Wolin, S.L. (1997) The yeast La protein is required for the 3′ endonucleolytic cleavage that matures tRNA precursors. Cell, 89, 393-402.
    • (1997) Cell , vol.89 , pp. 393-402
    • Yoo, C.J.1    Wolin, S.L.2
  • 39
    • 0026308783 scopus 로고
    • Efficient association of U2 snRNPs with pre-mRNA requires an essential U2 structural element
    • Zavanelli, M.I. and Ares, M., Jr (1991) Efficient association of U2 snRNPs with pre-mRNA requires an essential U2 structural element. Genes Dev., 5, 2521-2533.
    • (1991) Genes Dev. , vol.5 , pp. 2521-2533
    • Zavanelli, M.I.1    Ares Jr., M.2
  • 40
    • 0028349788 scopus 로고
    • Mutations in an essential U2 small nuclear RNA structure cause cold-sensitive U2 small nuclear ribonucleoprotein function by favoring competing alternative U2 RNA structures
    • Zavanelli, M.I., Britton, J.S., Igel, A.H. and Ares, M., Jr (1994) Mutations in an essential U2 small nuclear RNA structure cause cold-sensitive U2 small nuclear ribonucleoprotein function by favoring competing alternative U2 RNA structures. Mol. Cell. Biol., 14, 1689-1697.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1689-1697
    • Zavanelli, M.I.1    Britton, J.S.2    Igel, A.H.3    Ares Jr., M.4
  • 41
    • 0036163624 scopus 로고    scopus 로고
    • The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs
    • Zhang, A., Wassarman, K.M., Ortega, J., Steven, A.C. and Storz, G. (2002) The Sm-like Hfq protein increases OxyS RNA interaction with target mRNAs. Mol. Cell, 9, 11-22.
    • (2002) Mol. Cell , vol.9 , pp. 11-22
    • Zhang, A.1    Wassarman, K.M.2    Ortega, J.3    Steven, A.C.4    Storz, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.