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Volumn 62, Issue 4, 2006, Pages 1076-1089

Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 48; DNA PRIMASE; POLYPEPTIDE; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; RIBONUCLEASE; RNA; UNCLASSIFIED DRUG;

EID: 33750440205     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05393.x     Document Type: Article
Times cited : (43)

References (39)
  • 1
    • 23844442954 scopus 로고    scopus 로고
    • The 5S rRNA maturase, ribonuclease M5, is a Toprim domain family member
    • Allemand, F., Mathy, N., Brechemier-Baey, D., and Condon, C. (2005) The 5S rRNA maturase, ribonuclease M5, is a Toprim domain family member. Nucleic Acids Res 33: 4368-4376.
    • (2005) Nucleic Acids Res , vol.33 , pp. 4368-4376
    • Allemand, F.1    Mathy, N.2    Brechemier-Baey, D.3    Condon, C.4
  • 5
    • 0036529621 scopus 로고    scopus 로고
    • Comparative genomics and evolution of proteins involved in RNA metabolism
    • Anantharaman, V., Koonin, E.V., and Aravind, L. (2002) Comparative genomics and evolution of proteins involved in RNA metabolism. Nucleic Acids Res 30: 1427-1464.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1427-1464
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 6
    • 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
  • 7
    • 0034767932 scopus 로고    scopus 로고
    • Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosome
    • Baginsky, S., Shteiman-Kotler, A., Liveanu, V., Yehudai-Resheff, S., Bellaoui, M., Settlage, R.E. et al. (2001) Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosome. RNA 7: 1464-1475.
    • (2001) RNA , vol.7 , pp. 1464-1475
    • Baginsky, S.1    Shteiman-Kotler, A.2    Liveanu, V.3    Yehudai-Resheff, S.4    Bellaoui, M.5    Settlage, R.E.6
  • 8
    • 0030779484 scopus 로고    scopus 로고
    • Polyphosphate kinase is a component of the Escherichia coli RNA degradosome
    • Blum, E., Py, B., Carpousis, A.J., and Higgins, C.F. (1997) Polyphosphate kinase is a component of the Escherichia coli RNA degradosome. Mol Microbiol 26: 387-398.
    • (1997) Mol Microbiol , vol.26 , pp. 387-398
    • Blum, E.1    Py, B.2    Carpousis, A.J.3    Higgins, C.F.4
  • 9
    • 27644435644 scopus 로고    scopus 로고
    • Structural framework for the mechanism of archaeal exosomes in RNA processing
    • Büttner, K., Wenig, K., and Höpfner, 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
    • Büttner, K.1    Wenig, K.2    Höpfner, K.P.3
  • 10
    • 0344845397 scopus 로고    scopus 로고
    • The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis
    • Cao, K., Nakajima, R., Meyer, H.H., and Zheng, Y. (2003) The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell 115: 355-367.
    • (2003) Cell , vol.115 , pp. 355-367
    • Cao, K.1    Nakajima, R.2    Meyer, H.H.3    Zheng, Y.4
  • 11
    • 0028269435 scopus 로고
    • Copurification of E. coli RNAase E and PNPase: Evidence for a specific association between two enzymes important in RNA processing and degradation
    • Carpousis, A.J., Van Houwe, G., Ehretsmann, C., and Krisch, H.M. (1994) Copurification of E. coli RNAase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation. Cell 76: 889-900.
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J.1    Van Houwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 12
    • 0034693061 scopus 로고    scopus 로고
    • Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana rescues 5.8 S rRNA processing and mRNA decay defects of the yeast ski6 mutant and is found in an exosome-sized complex in plant and yeast cells
    • Chekanova, J.A., Shaw, R.J., Wills, M.A., and Belostotsky, D.A. (2000) Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana rescues 5.8 S rRNA processing and mRNA decay defects of the yeast ski6 mutant and is found in an exosome-sized complex in plant and yeast cells. J Biol Chem 275: 33158-33166.
    • (2000) J Biol Chem , vol.275 , pp. 33158-33166
    • Chekanova, J.A.1    Shaw, R.J.2    Wills, M.A.3    Belostotsky, D.A.4
  • 13
    • 0036464532 scopus 로고    scopus 로고
    • Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′->5′ exonuclease containing S1 and KH RNA-binding domains
    • Chekanova, J.A., Dutko, J.A., Mian, I.S., and Belostotsky, D.A. (2002) Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′->5′ exonuclease containing S1 and KH RNA-binding domains. Nucleic Acids Res 30: 695-700.
    • (2002) Nucleic Acids Res , vol.30 , pp. 695-700
    • Chekanova, J.A.1    Dutko, J.A.2    Mian, I.S.3    Belostotsky, D.A.4
  • 14
    • 0037977118 scopus 로고    scopus 로고
    • RNA processing and degradation in Bacillus subtilis
    • Condon, C. (2003) RNA processing and degradation in Bacillus subtilis. Microbiol Mol Biol Rev 67: 157-174.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 157-174
    • Condon, C.1
  • 15
    • 0032189582 scopus 로고    scopus 로고
    • Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli
    • Conrad, C., Rauhut, R., and Klug, G. (1998) Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli. Nucleic Acids Res 26: 4446-4453.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4446-4453
    • Conrad, C.1    Rauhut, R.2    Klug, G.3
  • 16
    • 0027380985 scopus 로고
    • RNase E activity is conferred by a single polypeptide: Overexpression, purification, and properties of the ams/rne/hmp1 gene product
    • Cormack, R.S., Genereaux, J.L., and Mackie, G.A. (1993) RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product. Proc Natl Acad Sci USA 90: 9006-9010.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9006-9010
    • Cormack, R.S.1    Genereaux, J.L.2    Mackie, G.A.3
  • 17
    • 0026660190 scopus 로고
    • Escherichia coli topoisomerase III-catalyzed cleavage of RNA
    • DiGate, R.J., and Marians, K.J. (1992) Escherichia coli topoisomerase III-catalyzed cleavage of RNA. J Biol Chem 267: 20532-20535.
    • (1992) J Biol Chem , vol.267 , pp. 20532-20535
    • DiGate, R.J.1    Marians, K.J.2
  • 18
    • 2242454128 scopus 로고    scopus 로고
    • Dehydrogenases from all three domains of life cleave RNA
    • Evguenieva-Hackenberg, E., Schiltz, E., and Klug, G. (2002) Dehydrogenases from all three domains of life cleave RNA. J Biol Chem 277: 46145-46150.
    • (2002) J Biol Chem , vol.277 , pp. 46145-46150
    • Evguenieva-Hackenberg, E.1    Schiltz, E.2    Klug, G.3
  • 20
    • 27644465196 scopus 로고    scopus 로고
    • Protein complexes in the archaeon Methanothermobacter thermautotrophicus analyzed by blue native/SDS-PAGE and mass spectrometry
    • Farhoud, M.H., Wessels, H.J., Steenbakkers, P.J., Mattijssen, S., Wevers, R.A., van Engelen, B.G., et al. (2005) Protein complexes in the archaeon Methanothermobacter thermautotrophicus analyzed by blue native/SDS-PAGE and mass spectrometry. Mol Cell Proteomics 4: 1653-1663.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1653-1663
    • Farhoud, M.H.1    Wessels, H.J.2    Steenbakkers, P.J.3    Mattijssen, S.4    Wevers, R.A.5    Van Engelen, B.G.6
  • 21
    • 0028905847 scopus 로고
    • Identification of an mRNA element promoting rate-limiting cleavage of the polycistronic puf mRNA in Rhodobacter capsulatus by an enzyme similar to RNase E
    • Fritsch, J., Rothfuchs, R., Rauhut, R., and Klug, G. (1995) Identification of an mRNA element promoting rate-limiting cleavage of the polycistronic puf mRNA in Rhodobacter capsulatus by an enzyme similar to RNase E. Mol Microbiol 15: 1017-1029.
    • (1995) Mol Microbiol , vol.15 , pp. 1017-1029
    • Fritsch, J.1    Rothfuchs, R.2    Rauhut, R.3    Klug, G.4
  • 22
    • 0028019612 scopus 로고
    • The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro
    • Guagliardi, A., Cerchia, L., Bartolucci, S., and Rossi, M. (1994) The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro. Protein Sci 3: 1436-1443.
    • (1994) Protein Sci , vol.3 , pp. 1436-1443
    • Guagliardi, A.1    Cerchia, L.2    Bartolucci, S.3    Rossi, M.4
  • 24
    • 0034745504 scopus 로고    scopus 로고
    • Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach
    • Koonin, E.V., Wolf, Y.I., and Aravind, L. (2001) Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach. Genome Res 11: 240-252.
    • (2001) Genome Res , vol.11 , pp. 240-252
    • Koonin, E.V.1    Wolf, Y.I.2    Aravind, L.3
  • 26
    • 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
  • 28
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase E in a multicomponent ribonucleolytic complex
    • Miczak, A., Kaberdin, V.R., Wei, C.L., and Lin-Chao, S. (1996) Proteins associated with RNase E in a multicomponent ribonucleolytic complex. Proc Natl Acad Sci USA 93: 3865-3869.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3865-3869
    • Miczak, A.1    Kaberdin, V.R.2    Wei, C.L.3    Lin-Chao, S.4
  • 29
    • 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., and Tollervey, D. (1997) The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′->5′ 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
  • 30
    • 28544443737 scopus 로고    scopus 로고
    • RNA polyadenylation in Archaea: Not observed in Haloferax while the exosome polynucleotidylates RNA in Sulfolobus
    • 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.
    • (2005) EMBO Rep , vol.6 , pp. 1188-1193
    • Portnoy, V.1    Evguenieva-Hackenberg, E.2    Klein, F.3    Walter, P.4    Lorentzen, E.5    Klug, G.6    Schuster, G.7
  • 31
    • 17644380001 scopus 로고    scopus 로고
    • Exoribonuclease R interacts with endoribonuclease E and an RNA-helicase in the psychrotrophic bacterium Pseudomonas syringe Lz4W
    • Purusharth, R.I., Klein, F., Sulthana, S., Jäger, S., Jagannadham, M.V., Evguenieva-Hackenberg, E., et al. (2005) Exoribonuclease R interacts with endoribonuclease E and an RNA-helicase in the psychrotrophic bacterium Pseudomonas syringe Lz4W. J Biol Chem 280: 14572-14578.
    • (2005) J Biol Chem , vol.280 , pp. 14572-14578
    • Purusharth, R.I.1    Klein, F.2    Sulthana, S.3    Jäger, S.4    Jagannadham, M.V.5    Evguenieva-Hackenberg, E.6
  • 32
    • 0036977391 scopus 로고    scopus 로고
    • Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring
    • Raijmakers, R., Egbarts, W.V., van Venrooij, W.J., and Pruijn, G.J. (2002) Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J Mol Biol 323: 653-663.
    • (2002) J Mol Biol , vol.323 , pp. 653-663
    • Raijmakers, R.1    Egbarts, W.V.2    Van Venrooij, W.J.3    Pruijn, G.J.4
  • 33
    • 4344573414 scopus 로고    scopus 로고
    • The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm
    • Raijmakers, R., Schilders, G., and Pruijn, G. (2004) The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm. Eur J Cell Biol 83: 175-183.
    • (2004) Eur J Cell Biol , vol.83 , pp. 175-183
    • Raijmakers, R.1    Schilders, G.2    Pruijn, G.3
  • 34
    • 33646591595 scopus 로고    scopus 로고
    • The Pyrococcus exosome complex: Structural and functional characterisation
    • Ramos, C.R., Oliveira, C.L., Torriani, I.L., and Oliveira, C.C. (2006) The Pyrococcus exosome complex: structural and functional characterisation. J Biol Chem 281: 6751-6759.
    • (2006) J Biol Chem , vol.281 , pp. 6751-6759
    • Ramos, C.R.1    Oliveira, C.L.2    Torriani, I.L.3    Oliveira, C.C.4
  • 35
    • 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
  • 37
    • 0036753399 scopus 로고    scopus 로고
    • A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription
    • Werner, F., and Weinzierl, R.O. (2002) A recombinant RNA polymerase II-like enzyme capable of promoter-specific transcription. Mol Cell 10: 635-646.
    • (2002) Mol Cell , vol.10 , pp. 635-646
    • Werner, F.1    Weinzierl, R.O.2
  • 38
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D., and Rapoport, T.A. (2004) A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol. Nature 429: 841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 39
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo, Y., and Deutscher, M.P. (2001) Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res 29: 1017-1026.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.