메뉴 건너뛰기




Volumn 5, Issue MAR, 2014, Pages

Non-stop mRNA decay: A special attribute of trans-translation mediated ribosome rescue

Author keywords

Non stop mRNA; Rnase R; SmpB; TmRNA; trans translation

Indexed keywords

ALANINE; AMINO ACID; ENZYME; MESSENGER RNA; NON STOP MRNA; RIBONUCLEASE R; UNCLASSIFIED DRUG;

EID: 84897951772     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00093     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • 2006 0008. doi: 10.1038/msb4100050
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., et al. (2006). Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006 0008. doi: 10.1038/msb4100050.
    • (2006) Mol. Syst. Biol. , vol.2
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 2
    • 84857768741 scopus 로고    scopus 로고
    • The tmRNA-tagging mechanism and the control of gene expression: a review
    • doi: 10.1002/wrna.48
    • Barends, S., Kraal, B., and van Wezel, G. P. (2011). The tmRNA-tagging mechanism and the control of gene expression: a review. Wiley Interdiscip. Rev. RNA 2, 233-246. doi: 10.1002/wrna.48.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 233-246
    • Barends, S.1    Kraal, B.2    van Wezel, G.P.3
  • 3
    • 83355166284 scopus 로고    scopus 로고
    • A tale of two mRNA degradation pathways mediated by RNase E
    • doi: 10.1111/j.1365-2958.2011.07894.x
    • Bouvier, M., and Carpousis, A. J. (2011). A tale of two mRNA degradation pathways mediated by RNase E. Mol. Microbiol. 82, 1305-1310. doi: 10.1111/j.1365-2958.2011.07894.x.
    • (2011) Mol. Microbiol. , vol.82 , pp. 1305-1310
    • Bouvier, M.1    Carpousis, A.J.2
  • 4
    • 84886928712 scopus 로고    scopus 로고
    • Active and accurate trans-translation requires distinct determinants in the C-terminal tail of SmpB protein and the mRNA-like domain of transfer messenger RNA (tmRNA)
    • doi: 10.1074/jbc.M113.503896
    • Camenares, D., Dulebohn, D. P., Svetlanov, A., and Karzai, A. W. (2013). Active and accurate trans-translation requires distinct determinants in the C-terminal tail of SmpB protein and the mRNA-like domain of transfer messenger RNA (tmRNA). J. Biol. Chem. 288, 30527-30542. doi: 10.1074/jbc.M113.503896.
    • (2013) J. Biol. Chem. , vol.288 , pp. 30527-30542
    • Camenares, D.1    Dulebohn, D.P.2    Svetlanov, A.3    Karzai, A.W.4
  • 5
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E
    • doi: 10.1146/annurev.micro.61.080706.093440
    • Carpousis, A. J. (2007). The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu. Rev. Microbiol. 61, 71-87. doi: 10.1146/annurev.micro.61.080706.093440.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 6
    • 84867044295 scopus 로고    scopus 로고
    • ArfA recruits release factor 2 to rescue stalled ribosomes by peptidyl-tRNA hydrolysis in Escherichia coli
    • doi: 10.1111/j.1365-2958.2012.08190.x
    • Chadani, Y., Ito, K., Kutsukake, K., and Abo, T. (2012). ArfA recruits release factor 2 to rescue stalled ribosomes by peptidyl-tRNA hydrolysis in Escherichia coli. Mol. Microbiol. 86, 37-50. doi: 10.1111/j.1365-2958.2012.08190.x.
    • (2012) Mol. Microbiol. , vol.86 , pp. 37-50
    • Chadani, Y.1    Ito, K.2    Kutsukake, K.3    Abo, T.4
  • 7
    • 79955008757 scopus 로고    scopus 로고
    • Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways
    • doi: 10.1111/j.1365-2958.2011.07607.x
    • Chadani, Y., Ono, K., Kutsukake, K., and Abo, T. (2011). Escherichia coli YaeJ protein mediates a novel ribosome-rescue pathway distinct from SsrA- and ArfA-mediated pathways. Mol. Microbiol. 80, 772-785. doi: 10.1111/j.1365-2958.2011.07607.x.
    • (2011) Mol. Microbiol. , vol.80 , pp. 772-785
    • Chadani, Y.1    Ono, K.2    Kutsukake, K.3    Abo, T.4
  • 8
    • 78349300881 scopus 로고    scopus 로고
    • Ribosome rescue by Escherichia coli ArfA (YhdL) in the absence of trans-translation system
    • doi: 10.1111/j.1365-2958.2010.07375.x
    • Chadani, Y., Ono, K., Ozawa, S., Takahashi, Y., Takai, K., Nanamiya, H., et al. (2010). Ribosome rescue by Escherichia coli ArfA (YhdL) in the absence of trans-translation system. Mol. Microbiol. 78, 796-808. doi: 10.1111/j.1365-2958.2010.07375.x.
    • (2010) Mol. Microbiol. , vol.78 , pp. 796-808
    • Chadani, Y.1    Ono, K.2    Ozawa, S.3    Takahashi, Y.4    Takai, K.5    Nanamiya, H.6
  • 9
    • 0037077311 scopus 로고    scopus 로고
    • Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II
    • doi: 10.1074/jbc.M202942200
    • Cheng, Z. F., and Deutscher, M. P. (2002). Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J. Biol. Chem. 277, 21624-21629. doi: 10.1074/jbc.M202942200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21624-21629
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 10
    • 0038652098 scopus 로고    scopus 로고
    • Quality control of ribosomal RNA mediated by polynucleotide phosphorylase and RNase R
    • doi: 10.1073/pnas.1231041100
    • Cheng, Z. F., and Deutscher, M. P. (2003). Quality control of ribosomal RNA mediated by polynucleotide phosphorylase and RNase R. Proc. Natl. Acad. Sci. U.S.A. 100, 6388-6393. doi: 10.1073/pnas.1231041100.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6388-6393
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 11
    • 34247519181 scopus 로고    scopus 로고
    • Trans-translation: the tmRNA-mediated surveillance mechanism for ribosome rescue, directed protein degradation, and nonstop mRNA decay
    • doi: 10.1021/bi6026055
    • Dulebohn, D., Choy, J., Sundermeier, T., Okan, N., and Karzai, A. W. (2007). Trans-translation: the tmRNA-mediated surveillance mechanism for ribosome rescue, directed protein degradation, and nonstop mRNA decay. Biochemistry 46, 4681-4693. doi: 10.1021/bi6026055.
    • (2007) Biochemistry , vol.46 , pp. 4681-4693
    • Dulebohn, D.1    Choy, J.2    Sundermeier, T.3    Okan, N.4    Karzai, A.W.5
  • 12
    • 33748414894 scopus 로고    scopus 로고
    • Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex
    • doi: 10.1038/nature05080
    • Frazao, C., McVey, C. E., Amblar, M., Barbas, A., Vonrhein, C., Arraiano, C. M., et al. (2006). Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex. Nature 443, 110-114. doi: 10.1038/nature05080.
    • (2006) Nature , vol.443 , pp. 110-114
    • Frazao, C.1    McVey, C.E.2    Amblar, M.3    Barbas, A.4    Vonrhein, C.5    Arraiano, C.M.6
  • 13
    • 78649617733 scopus 로고    scopus 로고
    • Non-stop mRNA decay initiates at the ribosome
    • doi: 10.1111/j.1365-2958.2010.07396.x
    • Ge, Z., Mehta, P., Richards, J., and Karzai, A. W. (2010). Non-stop mRNA decay initiates at the ribosome. Mol. Microbiol. 78, 1159-1170. doi: 10.1111/j.1365-2958.2010.07396.x.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1159-1170
    • Ge, Z.1    Mehta, P.2    Richards, J.3    Karzai, A.W.4
  • 14
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux tres petits angles; application a l'etude de phenomenes ultramicroscopiques
    • Guinier, A. (1939). La diffraction des rayons X aux tres petits angles; application a l'etude de phenomenes ultramicroscopiques. Ann. Phys. 12, 161-237.
    • (1939) Ann. Phys. , vol.12 , pp. 161-237
    • Guinier, A.1
  • 15
    • 71549151293 scopus 로고    scopus 로고
    • Beyond ribosome rescue: tmRNA and co-translational processes
    • doi: 10.1016/j.febslet.2009.11.023
    • Hayes, C. S., and Keiler, K. C. (2010). Beyond ribosome rescue: tmRNA and co-translational processes. FEBS Lett. 584, 413-419. doi: 10.1016/j.febslet.2009.11.023.
    • (2010) FEBS Lett. , vol.584 , pp. 413-419
    • Hayes, C.S.1    Keiler, K.C.2
  • 16
    • 22144462503 scopus 로고    scopus 로고
    • Cell cycle-regulated degradation of tmRNA is controlled by RNase R and SmpB
    • doi: 10.1111/j.1365-2958.2005.04709.x
    • Hong, S. J., Tran, Q. A., and Keiler, K. C. (2005). Cell cycle-regulated degradation of tmRNA is controlled by RNase R and SmpB. Mol. Microbiol. 57, 565-575. doi: 10.1111/j.1365-2958.2005.04709.x.
    • (2005) Mol. Microbiol. , vol.57 , pp. 565-575
    • Hong, S.J.1    Tran, Q.A.2    Keiler, K.C.3
  • 17
    • 84873465400 scopus 로고    scopus 로고
    • Conserved bacterial RNase YbeY plays key roles in 70S ribosome quality control and 16S rRNA maturation
    • doi: 10.1016/j.molcel.2012.11.025
    • Jacob, A. I., Kohrer, C., Davies, B. W., RajBhandary, U. L., and Walker, G. C. (2013). Conserved bacterial RNase YbeY plays key roles in 70S ribosome quality control and 16S rRNA maturation. Mol. Cell 49, 427-438. doi: 10.1016/j.molcel.2012.11.025.
    • (2013) Mol. Cell , vol.49 , pp. 427-438
    • Jacob, A.I.1    Kohrer, C.2    Davies, B.W.3    RajBhandary, U.L.4    Walker, G.C.5
  • 18
    • 0034046020 scopus 로고    scopus 로고
    • The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue
    • doi: 10.1038/75843
    • Karzai, A. W., Roche, E. D., and Sauer, R. T. (2000). The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue. Nat. Struct. Biol. 7, 449-455. doi: 10.1038/75843.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 449-455
    • Karzai, A.W.1    Roche, E.D.2    Sauer, R.T.3
  • 19
    • 0035853072 scopus 로고    scopus 로고
    • Protein factors associated with the SsrA.SmpB tagging and ribosome rescue complex
    • doi: 10.1073/pnas.051628298
    • Karzai, A. W., and Sauer, R. T. (2001). Protein factors associated with the SsrA.SmpB tagging and ribosome rescue complex. Proc. Natl. Acad. Sci. U.S.A. 98, 3040-3044. doi: 10.1073/pnas.051628298.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3040-3044
    • Karzai, A.W.1    Sauer, R.T.2
  • 20
    • 0345465673 scopus 로고    scopus 로고
    • SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)
    • doi: 10.1093/emboj/18.13.3793
    • Karzai, A. W., Susskind, M. M., and Sauer, R. T. (1999). SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA). EMBO J. 18, 3793-3799. doi: 10.1093/emboj/18.13.3793.
    • (1999) EMBO J. , vol.18 , pp. 3793-3799
    • Karzai, A.W.1    Susskind, M.M.2    Sauer, R.T.3
  • 21
    • 53849117142 scopus 로고    scopus 로고
    • Biology of trans-translation
    • doi: 10.1146/annurev.micro.62.081307.162948
    • Keiler, K. C. (2008). Biology of trans-translation. Annu. Rev. Microbiol. 62, 133-151. doi: 10.1146/annurev.micro.62.081307.162948.
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 133-151
    • Keiler, K.C.1
  • 22
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • doi: 10.1126/science.271.5251.990
    • Keiler, K. C., Waller, P. R., and Sauer, R. T. (1996). Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271, 990-993. doi: 10.1126/science.271.5251.990.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 23
    • 0141484613 scopus 로고    scopus 로고
    • PRIMUS: a Windows PC-based system for small-angle scattering data analysis
    • doi: 10.1107/S0021889803012779
    • Konarev, P. V., Volkov, V. V., Sokolova, A. V., Koch, M. H. J., and Svergun, D. I. (2003). PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J. Appl. Crystallogr. 36, 1277-1282. doi: 10.1107/S0021889803012779.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 1277-1282
    • Konarev, P.V.1    Volkov, V.V.2    Sokolova, A.V.3    Koch, M.H.J.4    Svergun, D.I.5
  • 24
    • 84866939617 scopus 로고    scopus 로고
    • Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases
    • doi: 10.1074/jbc.M112.375287
    • Liang, W., and Deutscher, M. P. (2012). Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases. J. Biol. Chem. 287, 33472-33479. doi: 10.1074/jbc.M112.375287.
    • (2012) J. Biol. Chem. , vol.287 , pp. 33472-33479
    • Liang, W.1    Deutscher, M.P.2
  • 25
    • 84861503555 scopus 로고    scopus 로고
    • The Small Angle Scattering ToolBox (SASTBX): an open-source software for biomolecular small-angle scattering
    • doi: 10.1107/S0021889812015786
    • Liu, H. G., Hexemer, A., and Zwart, P. H. (2012). The Small Angle Scattering ToolBox (SASTBX): an open-source software for biomolecular small-angle scattering. J. Appl. Crystallogr. 45, 587-593. doi: 10.1107/S0021889812015786.
    • (2012) J. Appl. Crystallogr. , vol.45 , pp. 587-593
    • Liu, H.G.1    Hexemer, A.2    Zwart, P.H.3
  • 26
    • 79955713801 scopus 로고    scopus 로고
    • Swapping the domains of exoribonucleases RNase II and RNase R: conferring upon RNase II the ability to degrade ds RNA
    • doi: 10.1002/prot.23010
    • Matos, R. G., Barbas, A., Gomez-Puertas, P., and Arraiano, C. M. (2011). Swapping the domains of exoribonucleases RNase II and RNase R: conferring upon RNase II the ability to degrade ds RNA. Proteins 79, 1853-1867. doi: 10.1002/prot.23010.
    • (2011) Proteins , vol.79 , pp. 1853-1867
    • Matos, R.G.1    Barbas, A.2    Gomez-Puertas, P.3    Arraiano, C.M.4
  • 27
    • 84864117764 scopus 로고    scopus 로고
    • Ribosome purification approaches for studying interactions of regulatory proteins and RNAs with the ribosome
    • doi: 10.1007/978-1-61779-949-5_18
    • Mehta, P., Woo, P., Venkataraman, K., and Karzai, A. W. (2012). Ribosome purification approaches for studying interactions of regulatory proteins and RNAs with the ribosome. Methods Mol. Biol. 905, 273-289. doi: 10.1007/978-1-61779-949-5_18.
    • (2012) Methods Mol. Biol. , vol.905 , pp. 273-289
    • Mehta, P.1    Woo, P.2    Venkataraman, K.3    Karzai, A.W.4
  • 28
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • doi: 10.1529/biophysj.105.064154
    • Petoukhov, M. V., and Svergun, D. I. (2005). Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89, 1237-1250. doi: 10.1529/biophysj.105.064154.
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 29
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution
    • doi: 10.1017/S0033583507004635
    • Putnam, C. D., Hammel, M., Hura, G. L., and Tainer, J. A. (2007). X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40, 191-285. doi: 10.1017/S0033583507004635.
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 30
    • 33751358590 scopus 로고    scopus 로고
    • RNase R degrades non-stop mRNAs selectively in an SmpB-tmRNA-dependent manner
    • doi: 10.1111/j.1365-2958.2006.05472.x
    • Richards, J., Mehta, P., and Karzai, A. W. (2006). RNase R degrades non-stop mRNAs selectively in an SmpB-tmRNA-dependent manner. Mol. Microbiol. 62, 1700-1712. doi: 10.1111/j.1365-2958.2006.05472.x.
    • (2006) Mol. Microbiol. , vol.62 , pp. 1700-1712
    • Richards, J.1    Mehta, P.2    Karzai, A.W.3
  • 31
    • 0026244044 scopus 로고
    • Gnom-a program package for small-angle scattering data-processing
    • doi: 10.1107/S002188989100081X
    • Semenyuk, A. V., and Svergun, D. I. (1991). Gnom-a program package for small-angle scattering data-processing. J. Appl. Crystallogr. 24, 537-540. doi: 10.1107/S002188989100081X.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 32
    • 58249090831 scopus 로고    scopus 로고
    • Studying tmRNA-mediated surveillance and nonstop mRNA decay
    • doi: 10.1016/S0076-6879(08)02217-9
    • Sundermeier, T., Ge, Z., Richards, J., Dulebohn, D., and Karzai, A. W. (2008). Studying tmRNA-mediated surveillance and nonstop mRNA decay. Methods Enzymol. 447, 329-358. doi: 10.1016/S0076-6879(08)02217-9.
    • (2008) Methods Enzymol. , vol.447 , pp. 329-358
    • Sundermeier, T.1    Ge, Z.2    Richards, J.3    Dulebohn, D.4    Karzai, A.W.5
  • 33
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • doi: 10.1016/S0006-3495(99)77443-6
    • Svergun, D. I. (1999). Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886. doi: 10.1016/S0006-3495(99)77443-6.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 34
    • 58649092877 scopus 로고    scopus 로고
    • The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA
    • doi: 10.1074/jbc.M806468200
    • Vincent, H. A., and Deutscher, M. P. (2009). The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA. J. Biol. Chem. 284, 486-494. doi: 10.1074/jbc.M806468200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 486-494
    • Vincent, H.A.1    Deutscher, M.P.2
  • 35
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • doi: 10.1107/S0021889803000268
    • Volkov, V. V., and Svergun, D. I. (2003). Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864. doi: 10.1107/S0021889803000268.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 36
    • 0242523959 scopus 로고    scopus 로고
    • A salvage pathway for protein structures: tmRNA and trans-translation
    • doi: 10.1146/annurev.micro.57.030502.090945
    • Withey, J. H., and Friedman, D. I. (2003). A salvage pathway for protein structures: tmRNA and trans-translation. Annu. Rev. Microbiol. 57, 101-123. doi: 10.1146/annurev.micro.57.030502.090945.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 101-123
    • Withey, J.H.1    Friedman, D.I.2
  • 37
    • 48649100966 scopus 로고    scopus 로고
    • Making the jump: new insights into the mechanism of trans-translation
    • doi: 10.1186/jbiol78
    • Wower, J., Wower, I. K., and Zwieb, C. (2008). Making the jump: new insights into the mechanism of trans-translation. J. Biol. 7, 17. doi: 10.1186/jbiol78.
    • (2008) J. Biol. , vol.7 , pp. 17
    • Wower, J.1    Wower, I.K.2    Zwieb, C.3
  • 38
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • doi: 10.1186/1471-2105-9-40
    • Zhang, Y. (2008). I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40. doi: 10.1186/1471-2105-9-40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 39
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: structural analysis and phylogenetic distribution
    • doi: 10.1093/nar/29.5.1017
    • Zuo, Y., and Deutscher, M. P. (2001). Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res. 29, 1017-1026. doi: 10.1093/nar/29.5.1017.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 40
    • 33749072017 scopus 로고    scopus 로고
    • Structural basis for processivity and single-strand specificity of RNase II
    • doi: 10.1016/j.molcel.2006.09.004
    • Zuo, Y., Vincent, H. A., Zhang, J., Wang, Y., Deutscher, M. P., and Malhotra, A. (2006). Structural basis for processivity and single-strand specificity of RNase II. Mol. Cell 24, 149-156. doi: 10.1016/j.molcel.2006.09.004.
    • (2006) Mol. Cell , vol.24 , pp. 149-156
    • Zuo, Y.1    Vincent, H.A.2    Zhang, J.3    Wang, Y.4    Deutscher, M.P.5    Malhotra, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.