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Volumn 13, Issue 2, 2004, Pages 225-239

High-Definition Macromolecular Composition of Yeast RNA-Processing Complexes

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL RNA; OLIGONUCLEOTIDE; POLYPEPTIDE;

EID: 10744227471     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00003-6     Document Type: Article
Times cited : (328)

References (67)
  • 4
    • 0033601196 scopus 로고    scopus 로고
    • The action of N-terminal actyltransferases on yeast ribosomal proteins
    • Arnold R.J., Polevodas B., Reilly J.P., Sherman F. The action of N-terminal actyltransferases on yeast ribosomal proteins. J. Biol. Chem. 274:1999;37035-37040.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37035-37040
    • Arnold, R.J.1    Polevodas, B.2    Reilly, J.P.3    Sherman, F.4
  • 5
    • 0032080005 scopus 로고    scopus 로고
    • Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a nontypical RNA binding element
    • Bagni C., Lapeyre B. Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a nontypical RNA binding element. J. Biol. Chem. 273:1998;10868-10873.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10868-10873
    • Bagni, C.1    Lapeyre, B.2
  • 7
    • 0030871663 scopus 로고    scopus 로고
    • Functional analysis of Rrp7p, an essential yeast protein involved in pre-rRNA processing and ribosome assembly
    • Baudin-Baillieu A., Tollervery D., Cullin C., Lacroute F. Functional analysis of Rrp7p, an essential yeast protein involved in pre-rRNA processing and ribosome assembly. Mol. Cell. Biol. 17:1997;5023-5032.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5023-5032
    • Baudin-Baillieu, A.1    Tollervery, D.2    Cullin, C.3    Lacroute, F.4
  • 9
    • 0034043398 scopus 로고    scopus 로고
    • Rrp8p is a yeast nucleolar protein functionally linked to Gar1p and involved in pre-rRNA cleavage at site A2
    • Bousquet-Antonelli C., Vanrobays E., Gelugne J.P., Caizergues-Ferrer, Henry Y. Rrp8p is a yeast nucleolar protein functionally linked to Gar1p and involved in pre-rRNA cleavage at site A2. RNA. 6:2000;826-843.
    • (2000) RNA , vol.6 , pp. 826-843
    • Bousquet-Antonelli, C.1    Vanrobays, E.2    Gelugne, J.P.3    Caizergues-Ferrer4    Henry, Y.5
  • 10
    • 0022764368 scopus 로고
    • Eukaryotic pre-tRNA 5′ processing nuclease: Copurification with a complex cylindrical particle
    • Castano J.G., Ornberg R., Koster J.G., Tobian J.A., Zasloff M. Eukaryotic pre-tRNA 5′ processing nuclease. copurification with a complex cylindrical particle Cell. 46:1986;377-387.
    • (1986) Cell , vol.46 , pp. 377-387
    • Castano, J.G.1    Ornberg, R.2    Koster, J.G.3    Tobian, J.A.4    Zasloff, M.5
  • 11
    • 0028226498 scopus 로고
    • PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae
    • Clausen M., Lamb C.J., Megnet R., Doerner P.W. PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae. Gene. 142:1994;107-112.
    • (1994) Gene , vol.142 , pp. 107-112
    • Clausen, M.1    Lamb, C.J.2    Megnet, R.3    Doerner, P.W.4
  • 12
    • 0029775561 scopus 로고    scopus 로고
    • The yeast splicing factor Mud13p is a commitment complex component and corresponds to Cbp20, the small subunit of the nuclear cap-binding complex
    • Colot H.V., Stutz F., Rosbash M. The yeast splicing factor Mud13p is a commitment complex component and corresponds to Cbp20, the small subunit of the nuclear cap-binding complex. Genes Dev. 10:1996;1699-1708.
    • (1996) Genes Dev. , vol.10 , pp. 1699-1708
    • Colot, H.V.1    Stutz, F.2    Rosbash, M.3
  • 13
    • 0028883820 scopus 로고
    • The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo
    • DeMarini D.J., Papa F.R., Swaminathan S., Ursic D., Rasmussen T.P., Culbertson M.R., Hochstrasser M. The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo. Mol. Cell. Biol. 15:1995;6311-6321.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6311-6321
    • Demarini, D.J.1    Papa, F.R.2    Swaminathan, S.3    Ursic, D.4    Rasmussen, T.P.5    Culbertson, M.R.6    Hochstrasser, M.7
  • 14
    • 0034707668 scopus 로고    scopus 로고
    • Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles
    • Dostie J., Lejbkowicz F., Sonenberg N. Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles. J. Cell Biol. 148:2000;239-245.
    • (2000) J. Cell Biol. , vol.148 , pp. 239-245
    • Dostie, J.1    Lejbkowicz, F.2    Sonenberg, N.3
  • 16
    • 0037188922 scopus 로고    scopus 로고
    • Yph1p, an ORC-interacting protein: Potential links between cell proliferation control, DNA replication, and ribosome biogenesis
    • Du Y.C., Stillman B. Yph1p, an ORC-interacting protein. potential links between cell proliferation control, DNA replication, and ribosome biogenesis Cell. 109:2002;835-848.
    • (2002) Cell , vol.109 , pp. 835-848
    • Du, Y.C.1    Stillman, B.2
  • 19
    • 0027102212 scopus 로고
    • Sit4 protein phosphatase is required for the normal accumulation of SWI4, CLN1, CLN2, and HCS26 RNAs during late G1
    • Fernandez-Sarabia M.J., Sutton A., Zhong T., Arndt K.T. Sit4 protein phosphatase is required for the normal accumulation of SWI4, CLN1, CLN2, and HCS26 RNAs during late G1. Genes Dev. 6:1992;2417-2428.
    • (1992) Genes Dev. , vol.6 , pp. 2417-2428
    • Fernandez-Sarabia, M.J.1    Sutton, A.2    Zhong, T.3    Arndt, K.T.4
  • 30
    • 0035839002 scopus 로고    scopus 로고
    • Coupled transcription and translation within nuclei of mammalian cells
    • Iborra F.J., Jackson D.A., Cook P.R. Coupled transcription and translation within nuclei of mammalian cells. Science. 293:2001;1139-1142.
    • (2001) Science , vol.293 , pp. 1139-1142
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 32
    • 0035702842 scopus 로고    scopus 로고
    • Brix from Xenopus laevis and Brx1p from yeast define a new family of proteins involved in the biogenesis of large ribosomal subunits
    • Kaser A., Bogengruber E., Hallegger M., Doppler E., Lepperdinger G., Jantsch M., Breitenbach M., Kreil G. Brix from Xenopus laevis and Brx1p from yeast define a new family of proteins involved in the biogenesis of large ribosomal subunits. Biol. Chem. 382:2001;1637-1647.
    • (2001) Biol. Chem. , vol.382 , pp. 1637-1647
    • Kaser, A.1    Bogengruber, E.2    Hallegger, M.3    Doppler, E.4    Lepperdinger, G.5    Jantsch, M.6    Breitenbach, M.7    Kreil, G.8
  • 33
    • 0343517443 scopus 로고    scopus 로고
    • Synthetic lethality with conditional dbp6 alleles identifies Rsa1p, a nucleoplasmic protein involved in the assembly of 60S ribosomal subunits
    • a
    • Kressler D., Doere M., Rojo M., Linder P. Synthetic lethality with conditional dbp6 alleles identifies Rsa1p, a nucleoplasmic protein involved in the assembly of 60S ribosomal subunits. Mol. Cell. Biol. 19:1999;8633-8645. a.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8633-8645
    • Kressler, D.1    Doere, M.2    Rojo, M.3    Linder, P.4
  • 34
    • 0033509092 scopus 로고    scopus 로고
    • Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae
    • b
    • Kressler D., Linder P., de La Cruz J. Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:1999;7897-7912. b.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7897-7912
    • Kressler, D.1    Linder, P.2    De La Cruz, J.3
  • 36
    • 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.J., Tollervey D. Precursors to the U3 small nucleolar RNA lack small nucleolar RNP proteins but are stabilized by La binding. Mol. Cell. Biol. 20:2000;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.J.5    Tollervey, D.6
  • 37
    • 0036288630 scopus 로고    scopus 로고
    • Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with the La-homologous protein Lhp1p
    • Kufel J., Allmang C., Verdone L., Beggs J.D., Tollervey D. Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with the La-homologous protein Lhp1p. Mol. Cell. Biol. 22:2002;5248-5256.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5248-5256
    • Kufel, J.1    Allmang, C.2    Verdone, L.3    Beggs, J.D.4    Tollervey, D.5
  • 38
    • 0036829415 scopus 로고    scopus 로고
    • Intron status and 3′-end formation control cotranscriptional export of mRNA
    • Lei E.P., Silver P.A. Intron status and 3′-end formation control cotranscriptional export of mRNA. Genes Dev. 16:2002;2761-2766.
    • (2002) Genes Dev. , vol.16 , pp. 2761-2766
    • Lei, E.P.1    Silver, P.A.2
  • 39
    • 0029790606 scopus 로고    scopus 로고
    • A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing
    • Lewis J.D., Gorlich D., Mattaj I.W. A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing. Nucleic Acids Res. 24:1996;3332-3336.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3332-3336
    • Lewis, J.D.1    Gorlich, D.2    Mattaj, I.W.3
  • 40
    • 0030929129 scopus 로고    scopus 로고
    • The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein
    • Liang W.Q., Clark J.A., Fournier M.J. The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein. Mol. Cell. Biol. 17:1997;4124-4132.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4124-4132
    • Liang, W.Q.1    Clark, J.A.2    Fournier, M.J.3
  • 41
    • 0030024350 scopus 로고    scopus 로고
    • Interaction between the U1 snRNP-A protein and the 160-kD subunit of cleavage-polyadenylation specificity factor increases polyadenylation efficiency in vitro
    • Lutz C.S., Murthy K.G., Scek N., O'Conner J.P., Manley J.L., Alwine J.C. Interaction between the U1 snRNP-A protein and the 160-kD subunit of cleavage-polyadenylation specificity factor increases polyadenylation efficiency in vitro. Genes Dev. 10:1996;325-337.
    • (1996) Genes Dev. , vol.10 , pp. 325-337
    • Lutz, C.S.1    Murthy, K.G.2    Scek, N.3    O'Conner, J.P.4    Manley, J.L.5    Alwine, J.C.6
  • 42
    • 0034006634 scopus 로고    scopus 로고
    • Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but not the mitochondrial Rnase P function of the Saccharomyces cerevisiae gene RPM2
    • Lutz M.S., Ellis S.R., Martin N.C. Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but not the mitochondrial Rnase P function of the Saccharomyces cerevisiae gene RPM2. Genetics. 154:2000;1013-1023.
    • (2000) Genetics , vol.154 , pp. 1013-1023
    • Lutz, M.S.1    Ellis, S.R.2    Martin, N.C.3
  • 43
    • 0033046012 scopus 로고    scopus 로고
    • Pseudouridine mapping in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (snRNAs) reveals that pseudouridine synthase Pus1p exhibits a dual substrate specificity for U2 snRNA and tRNA
    • Massenet S., Motorin Y., Lafontaine D.L.J., Hurt E.C., Grosjean H., Branlant C. Pseudouridine mapping in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (snRNAs) reveals that pseudouridine synthase Pus1p exhibits a dual substrate specificity for U2 snRNA and tRNA. Mol. Cell. Biol. 19:1999;2142-2154.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2142-2154
    • Massenet, S.1    Motorin, Y.2    Lafontaine, D.L.J.3    Hurt, E.C.4    Grosjean, H.5    Branlant, C.6
  • 45
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′-5′ exoribonucleases
    • Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D. The exosome. a conserved eukaryotic RNA processing complex containing multiple 3′-5′ exoribonucleases Cell. 91:1997;457-466.
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 46
    • 18644372079 scopus 로고    scopus 로고
    • 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm
    • Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E. 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm. EMBO J. 21:2002;5539-5547.
    • (2002) EMBO J. , vol.21 , pp. 5539-5547
    • Nissan, T.A.1    Bassler, J.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 49
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Seraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17:1999;1030-1032.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 51
    • 0026478895 scopus 로고
    • NOP3 is an essential yeast protein which is required for pre-rRNA processing
    • Russell I.D., Tollervey D. NOP3 is an essential yeast protein which is required for pre-rRNA processing. J. Cell Biol. 119:1992;737-747.
    • (1992) J. Cell Biol. , vol.119 , pp. 737-747
    • Russell, I.D.1    Tollervey, D.2
  • 52
    • 0029836594 scopus 로고    scopus 로고
    • TFIIS binds to mouse RNA polymerase I and stimulates transcript elongation and hydrolytic cleavage of nascent rRNA
    • Schnapp G., Graveley B.R., Grummt I. TFIIS binds to mouse RNA polymerase I and stimulates transcript elongation and hydrolytic cleavage of nascent rRNA. Mol. Gen. Genet. 252:1996;412-419.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 412-419
    • Schnapp, G.1    Graveley, B.R.2    Grummt, I.3
  • 54
    • 0037047107 scopus 로고    scopus 로고
    • The fifth essential DNA polymerase φ in Saccharomyces cerevisiae is localized to the nucleolus and plays an important role in synthesis or rRNA
    • Shimizu K., Kawasaki Y., Hiraga S.I., Tawaramoto M., Nakashima N., Sugino A. The fifth essential DNA polymerase φ in Saccharomyces cerevisiae is localized to the nucleolus and plays an important role in synthesis or rRNA. Proc. Natl. Acad. Sci. USA. 99:2002;9133-9138.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9133-9138
    • Shimizu, K.1    Kawasaki, Y.2    Hiraga, S.I.3    Tawaramoto, M.4    Nakashima, N.5    Sugino, A.6
  • 56
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal w. improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 57
    • 0037444342 scopus 로고    scopus 로고
    • The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo
    • Valasek L., Mathew A.A., Shin B.S., Nielsen K.H., Szamecz B., Hinnebusch A.G. The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev. 17:2003;786-799.
    • (2003) Genes Dev. , vol.17 , pp. 786-799
    • Valasek, L.1    Mathew, A.A.2    Shin, B.S.3    Nielsen, K.H.4    Szamecz, B.5    Hinnebusch, A.G.6
  • 58
    • 0029618257 scopus 로고
    • Processing of pre-ribosomal RNA in Saccharomyces cerevisiae
    • Venema J., Tollervey D. Processing of pre-ribosomal RNA in Saccharomyces cerevisiae. Yeast. 11:1995;1629-1650.
    • (1995) Yeast , vol.11 , pp. 1629-1650
    • Venema, J.1    Tollervey, D.2
  • 59
    • 0029853905 scopus 로고    scopus 로고
    • RRP5 is required for formation of both 18S and 5.8S rRNA in yeast
    • Venema J., Tollervey D. RRP5 is required for formation of both 18S and 5.8S rRNA in yeast. EMBO J. 15:1996;5701-5714.
    • (1996) EMBO J. , vol.15 , pp. 5701-5714
    • Venema, J.1    Tollervey, D.2
  • 60
    • 0033730378 scopus 로고    scopus 로고
    • Yeast Rrp9p is an evolutionarily conserved U3 snoRNP protein essential for early pre-rRNA processing cleavages and requires box C for its association
    • Venema J., Harman R.V., Faber A.W., Venrooij W.J.V., Raue H.A. Yeast Rrp9p is an evolutionarily conserved U3 snoRNP protein essential for early pre-rRNA processing cleavages and requires box C for its association. RNA. 6:2000;1660-1671.
    • (2000) RNA , vol.6 , pp. 1660-1671
    • Venema, J.1    Harman, R.V.2    Faber, A.W.3    Venrooij, W.J.V.4    Raue, H.A.5
  • 62
    • 0031016682 scopus 로고    scopus 로고
    • Dbp3p, a putative RNA helicase in Saccharomyces cerevisiae, is required for efficient pre-rRNA processing predominantly at site A3
    • Weaver P.L., Sun C., Chang T.H. Dbp3p, a putative RNA helicase in Saccharomyces cerevisiae, is required for efficient pre-rRNA processing predominantly at site A3. Mol. Cell. Biol. 17:1997;1354-1365.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1354-1365
    • Weaver, P.L.1    Sun, C.2    Chang, T.H.3
  • 63
    • 0347647733 scopus 로고    scopus 로고
    • Protein kinases CKI and CKII are implicated in modification of ribosomal proteins of the yeast Trichosporon cutaneum
    • Wojda I., Cytrynska M., Frajnt M.F., Jakubowicz T. Protein kinases CKI and CKII are implicated in modification of ribosomal proteins of the yeast Trichosporon cutaneum. Acta Biochim. Pol. 49:2002;947-957.
    • (2002) Acta Biochim. Pol. , vol.49 , pp. 947-957
    • Wojda, I.1    Cytrynska, M.2    Frajnt, M.F.3    Jakubowicz, T.4
  • 64
    • 0035878889 scopus 로고    scopus 로고
    • Nucleolar protein Nop12p participates in synthesis of 25S rRNA in Saccharomyces cerevisiae
    • Wu K., Wu P., Aris J.P. Nucleolar protein Nop12p participates in synthesis of 25S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res. 29:2001;2938-2949.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2938-2949
    • Wu, K.1    Wu, P.2    Aris, J.P.3
  • 65
    • 0036649020 scopus 로고    scopus 로고
    • Large-scale prediction of Saccharomyces cerevisiae gene function using overlapping transcriptional clusters
    • Wu L.F., Hughes T.R., Davierwala A.P., Robinson M.D., Stoughton R., Altschuler S.J. Large-scale prediction of Saccharomyces cerevisiae gene function using overlapping transcriptional clusters. Nat. Genet. 31:2002;255-265.
    • (2002) Nat. Genet. , vol.31 , pp. 255-265
    • Wu, L.F.1    Hughes, T.R.2    Davierwala, A.P.3    Robinson, M.D.4    Stoughton, R.5    Altschuler, S.J.6
  • 66
    • 0028109602 scopus 로고
    • Nucleolar proteins that bind NLSs: A role in nuclear import or ribosome biogenesis?
    • Xue Z., Melese T. Nucleolar proteins that bind NLSs. a role in nuclear import or ribosome biogenesis? Trends Cell Biol. 4:1994;414-417.
    • (1994) Trends Cell Biol. , vol.4 , pp. 414-417
    • Xue, Z.1    Melese, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.