메뉴 건너뛰기




Volumn 37, Issue 1, 2009, Pages 83-87

Lessons from structural and biochemical studies on the archaeal exosome

Author keywords

Archaeon; Exonuclease; Exosome; Helicase; Polyadenylation; RNA degradation

Indexed keywords

EXONUCLEASE; HELICASE; NUCLEASE; NUCLEOSIDE DIPHOSPHATASE; RIBONUCLEASE; ARCHAEAL RNA;

EID: 59749088456     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0370083     Document Type: Article
Times cited : (13)

References (35)
  • 2
    • 0027214097 scopus 로고
    • Yeast cells lacking 5′→3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure
    • Hsu, C.L. and Stevens, A. (1993) Yeast cells lacking 5′→3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure. Mol. Cell. Biol. 13, 4826-4835
    • (1993) Mol. Cell. Biol , vol.13 , pp. 4826-4835
    • Hsu, C.L.1    Stevens, A.2
  • 3
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 5′→3′ exoribonucleases
    • Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M. and Tollervey, D. (1997) The exosome: a conserved eukaryotic RNA processing complex containing multiple 5′→3′ exoribonucleases. Cell 91, 457-466
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 6
    • 0037180825 scopus 로고    scopus 로고
    • The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila
    • Andrulis, E.D., Werner, J., Nazarian, A., Erdjument-Bromage, H., Tempst, P. and Lis, J.T. (2002) The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature 420, 837-841
    • (2002) Nature , vol.420 , pp. 837-841
    • Andrulis, E.D.1    Werner, J.2    Nazarian, A.3    Erdjument-Bromage, H.4    Tempst, P.5    Lis, J.T.6
  • 7
    • 0035807308 scopus 로고    scopus 로고
    • Quality control of mRNA 3′-end processing is linked to the nuclear exosome
    • Hilleren, P., McCarthy, T., Rosbash, M., Parker, R. and Jensen, T.H. (2001) Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature 413, 538-542
    • (2001) Nature , vol.413 , pp. 538-542
    • Hilleren, P.1    McCarthy, T.2    Rosbash, M.3    Parker, R.4    Jensen, T.H.5
  • 8
    • 15444368560 scopus 로고    scopus 로고
    • Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome
    • Orban, T.I. and Izaurralde, E. (2005) Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome. RNA 11, 459-469
    • (2005) RNA , vol.11 , pp. 459-469
    • Orban, T.I.1    Izaurralde, E.2
  • 9
    • 0034975301 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae small GTPase, Gsp1p/Ran, is involved in 3′ processing of 7S-to-5.8S rRNA and in degradation of the excised 5′-A0 fragment of 35S pre-rRNA, both of which are carried out by the exosome
    • Suzuki, N., Noguchi, E., Nakashima, N., Oki, M., Ohba, T., Tartakoff, A., Ohishi, M. and Nishimoto, T. (2001) The Saccharomyces cerevisiae small GTPase, Gsp1p/Ran, is involved in 3′ processing of 7S-to-5.8S rRNA and in degradation of the excised 5′-A0 fragment of 35S pre-rRNA, both of which are carried out by the exosome. Genetics 158, 613-625
    • (2001) Genetics , vol.158 , pp. 613-625
    • Suzuki, N.1    Noguchi, E.2    Nakashima, N.3    Oki, M.4    Ohba, T.5    Tartakoff, A.6    Ohishi, M.7    Nishimoto, T.8
  • 10
    • 0035983990 scopus 로고    scopus 로고
    • Processing of 3′-extended read-through transcripts by the exosome can generate functional mRNAs
    • Torchet, C., Bousquet-Antonelli, C., Milligan, L., Thompson, E., Kufel, J. and Tollervey, D. (2002) Processing of 3′-extended read-through transcripts by the exosome can generate functional mRNAs. Mol. Cell 9, 1285-1296
    • (2002) Mol. Cell , vol.9 , pp. 1285-1296
    • Torchet, C.1    Bousquet-Antonelli, C.2    Milligan, L.3    Thompson, E.4    Kufel, J.5    Tollervey, D.6
  • 11
    • 0033981301 scopus 로고    scopus 로고
    • Yeast exosome mutants accumulate 3′-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs
    • van Hoof, A., Lennertz, P. and Parker, R. (2000) Yeast exosome mutants accumulate 3′-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs. Mol. Cell. Biol. 20, 441-452
    • (2000) Mol. Cell. Biol , vol.20 , pp. 441-452
    • van Hoof, A.1    Lennertz, P.2    Parker, R.3
  • 13
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons, M.F., Jones, G.H. and Luisi, B.F. (2000) A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure 8, 1215-1226
    • (2000) Structure , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 14
    • 27644435644 scopus 로고    scopus 로고
    • Structural framework for the mechanism of archaeal exosomes in RNA processing
    • Buttner, K., Wenig, K. and Hopfner, K.-P. (2005) Structural framework for the mechanism of archaeal exosomes in RNA processing. Mol. Cell 20, 461-471
    • (2005) Mol. Cell , vol.20 , pp. 461-471
    • Buttner, K.1    Wenig, K.2    Hopfner, K.-P.3
  • 16
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Liu, Q., Greimann, J.C. and Lima, C.D. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127, 1223-1237
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 17
    • 33846030499 scopus 로고    scopus 로고
    • Structural and biochemical characterization of the yeast exosome component Rrp40
    • Oddone, A., Lorentzen, E., Basquin, J., Gasch, A., Rybin, V., Conti, E. and Sattler, M. (2007) Structural and biochemical characterization of the yeast exosome component Rrp40. EMBO Rep. 8, 63-69
    • (2007) EMBO Rep , vol.8 , pp. 63-69
    • Oddone, A.1    Lorentzen, E.2    Basquin, J.3    Gasch, A.4    Rybin, V.5    Conti, E.6    Sattler, M.7
  • 19
    • 46649091980 scopus 로고    scopus 로고
    • Insights into the mechanism of progressive RNA degradation by the archaeal exosome
    • Navarro, M.V., Oliveira, C.C., Zanchin, N.I. and Guimaraes, B.G. (2008) Insights into the mechanism of progressive RNA degradation by the archaeal exosome. J. Biol. Chem. 283, 14120-14131
    • (2008) J. Biol. Chem , vol.283 , pp. 14120-14131
    • Navarro, M.V.1    Oliveira, C.C.2    Zanchin, N.I.3    Guimaraes, B.G.4
  • 20
    • 0000577868 scopus 로고    scopus 로고
    • The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex
    • Anderson, J.S. and Parker, R.P. (1998) The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex. EMBO J. 17, 1497-1506
    • (1998) EMBO J , vol.17 , pp. 1497-1506
    • Anderson, J.S.1    Parker, R.P.2
  • 21
    • 41949126822 scopus 로고    scopus 로고
    • Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3′→5′ helicase partner of the nuclear exosome
    • Bernstein, J., Patterson, D.N., Wilson, G.M. and Toth, E.A. (2008) Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3′→5′ helicase partner of the nuclear exosome. J. Biol. Chem. 283, 4930-4942
    • (2008) J. Biol. Chem , vol.283 , pp. 4930-4942
    • Bernstein, J.1    Patterson, D.N.2    Wilson, G.M.3    Toth, E.A.4
  • 25
    • 21444447661 scopus 로고    scopus 로고
    • Archaeal Hel308 helicase targets replication forks in vivo and in vitro and unwinds lagging strands
    • Guy, C.P. and Bolt, E.L. (2005) Archaeal Hel308 helicase targets replication forks in vivo and in vitro and unwinds lagging strands. Nucleic Acids Res. 33, 3678-3690
    • (2005) Nucleic Acids Res , vol.33 , pp. 3678-3690
    • Guy, C.P.1    Bolt, E.L.2
  • 26
    • 41949135245 scopus 로고    scopus 로고
    • Hjm/Hel308A DNA helicase from Sulfolobus tokodaii promotes replication fork regression and interacts with Hjc endonuclease in vitro
    • Li, Z., Lu, S., Hou, G., Ma, X., Sheng, D., Ni, J. and Shen, Y. (2008) Hjm/Hel308A DNA helicase from Sulfolobus tokodaii promotes replication fork regression and interacts with Hjc endonuclease in vitro. J. Bacteriol. 190, 3006-3017
    • (2008) J. Bacteriol , vol.190 , pp. 3006-3017
    • Li, Z.1    Lu, S.2    Hou, G.3    Ma, X.4    Sheng, D.5    Ni, J.6    Shen, Y.7
  • 27
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • Buttner, K., Nehring, S. and Hopfner, K.-P. (2007) Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat. Struct. Mol. Biol. 14, 647-652
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 647-652
    • Buttner, K.1    Nehring, S.2    Hopfner, K.-P.3
  • 28
    • 29844458585 scopus 로고    scopus 로고
    • Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome
    • Egecioglu, D.E., Henras, A.K. and Chanfreau, G.F. (2006) Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome. RNA 12, 26-32
    • (2006) RNA , vol.12 , pp. 26-32
    • Egecioglu, D.E.1    Henras, A.K.2    Chanfreau, G.F.3
  • 29
    • 33645739358 scopus 로고    scopus 로고
    • Yeast Trf5p is a nuclear poly(A) polymerase
    • Houseley, J. and Tollervey, D. (2006) Yeast Trf5p is a nuclear poly(A) polymerase. EMBO Rep. 7, 205-211
    • (2006) EMBO Rep , vol.7 , pp. 205-211
    • Houseley, J.1    Tollervey, D.2
  • 31
    • 27644496002 scopus 로고    scopus 로고
    • Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core
    • Lorentzen, E. and Conti, E. (2005) Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core. Mol. Cell 20, 473-481
    • (2005) Mol. Cell , vol.20 , pp. 473-481
    • Lorentzen, E.1    Conti, E.2
  • 32
    • 33846068920 scopus 로고    scopus 로고
    • A single subunit, Dis3, is essentially responsible for yeast exosome core activity
    • Dziembowski, A., Lorentzen, E., Conti, E. and Seraphin, B. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat. Struct. Mol. Biol. 14, 15-22
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 15-22
    • Dziembowski, A.1    Lorentzen, E.2    Conti, E.3    Seraphin, B.4
  • 33
    • 28544443737 scopus 로고    scopus 로고
    • Portnoy, V., Evguenieva-Hackenberg, E., Klein, F., Walter, P., Lorentzen, E., Klug, G. and Schuster, G. (2005) RNA polyadenylation in Archaea: not observed in Haloferax while the exosome polynucleotidylates RNA in Sulfolobus. EMBO Rep. 6, 1188-1193
    • Portnoy, V., Evguenieva-Hackenberg, E., Klein, F., Walter, P., Lorentzen, E., Klug, G. and Schuster, G. (2005) RNA polyadenylation in Archaea: not observed in Haloferax while the exosome polynucleotidylates RNA in Sulfolobus. EMBO Rep. 6, 1188-1193
  • 35
    • 40849106786 scopus 로고    scopus 로고
    • Structure of the active subunit of the yeast exosome core, Rrp44: Diverse modes of substrate recruitment in the RNase II nuclease family
    • Lorentzen, E., Basquin, J., Tomecki, R., Dziembowski, A. and Conti, E. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol. Cell 29, 717-728
    • (2008) Mol. Cell , vol.29 , pp. 717-728
    • Lorentzen, E.1    Basquin, J.2    Tomecki, R.3    Dziembowski, A.4    Conti, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.