메뉴 건너뛰기




Volumn 7, Issue 5, 2012, Pages

Fret-based identification of mRNAs undergoing translation

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RIBOSOMAL PROTEIN L1; TRANSFER RNA; FLUORESCENT DYE; RIBOSOME PROTEIN;

EID: 84861654080     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0038344     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 33646106593 scopus 로고    scopus 로고
    • Measurement of protein turnover rates by heavy water labeling of nonessential amino acids
    • Busch R, Kim YK, Neese RA, Schade-Serin V, Collins M, et al. (2006) Measurement of protein turnover rates by heavy water labeling of nonessential amino acids. Biochim Biophys Acta 1760: 730-744.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 730-744
    • Busch, R.1    Kim, Y.K.2    Neese, R.A.3    Schade-Serin, V.4    Collins, M.5
  • 2
    • 62549134121 scopus 로고    scopus 로고
    • Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
    • Ingolia NT, Ghaemmaghami S, Newman JRS, Weissman JS, (2009) Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324: 218-223.
    • (2009) Science , vol.324 , pp. 218-223
    • Ingolia, N.T.1    Ghaemmaghami, S.2    Newman, J.R.S.3    Weissman, J.S.4
  • 3
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • Lippincott-Schwartz J, Patterson GH, (2003) Development and use of fluorescent protein markers in living cells. Science 300: 87-91.
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 5
    • 33845257870 scopus 로고    scopus 로고
    • Variability and memory of protein levels in human cells
    • Sigal A, Milo R, Cohen A, Geva-Zatorsky N, Klein Y, et al. (2006) Variability and memory of protein levels in human cells. Nature 444: 643-646.
    • (2006) Nature , vol.444 , pp. 643-646
    • Sigal, A.1    Milo, R.2    Cohen, A.3    Geva-Zatorsky, N.4    Klein, Y.5
  • 6
    • 57149121357 scopus 로고    scopus 로고
    • Determination of protein by synchronous fluorometric method with a new indole homodimeric cyanine as fluorescence probe
    • Lin XC, Yan J, Guo LQ, Xie ZH, (2008) Determination of protein by synchronous fluorometric method with a new indole homodimeric cyanine as fluorescence probe. Spectroscopy and Spectral Analysis 28: 2615-2618.
    • (2008) Spectroscopy and Spectral Analysis , vol.28 , pp. 2615-2618
    • Lin, X.C.1    Yan, J.2    Guo, L.Q.3    Xie, Z.H.4
  • 7
    • 77954633083 scopus 로고    scopus 로고
    • A fluorophore ligase for site-specific protein labeling inside living cells
    • Uttamapinant C, White KA, Baruah H, Thompson S, Fernandez-Suarez M, et al. (2010) A fluorophore ligase for site-specific protein labeling inside living cells. PNAS 107: 10914-10919.
    • (2010) PNAS , vol.107 , pp. 10914-10919
    • Uttamapinant, C.1    White, K.A.2    Baruah, H.3    Thompson, S.4    Fernandez-Suarez, M.5
  • 8
    • 3042826388 scopus 로고    scopus 로고
    • In vivo targeting of organic calcium sensors via genetically selected peptides
    • Marks KM, Rosinov M, Nolan GP, (2004) In vivo targeting of organic calcium sensors via genetically selected peptides. Chem Biol 11: 347-356.
    • (2004) Chem Biol , vol.11 , pp. 347-356
    • Marks, K.M.1    Rosinov, M.2    Nolan, G.P.3
  • 9
    • 58949092972 scopus 로고    scopus 로고
    • Site-specific covalent labeling of proteins inside live cells using small molecule probes
    • Chattopadhaya S, Srinivasan R, Yeo DSY, Chen GYJ, Yao SQ, (2009) Site-specific covalent labeling of proteins inside live cells using small molecule probes. Bioorg Med Chem 17: 981-989.
    • (2009) Bioorg Med Chem , vol.17 , pp. 981-989
    • Chattopadhaya, S.1    Srinivasan, R.2    Yeo, D.S.Y.3    Chen, G.Y.J.4    Yao, S.Q.5
  • 10
    • 77951107295 scopus 로고    scopus 로고
    • Real-time tRNA transit on single translating ribosomes at codon resolution
    • Uemura S, Aitken CE, Korlach J, Flusberg BA, Turner SW, et al. (2010) Real-time tRNA transit on single translating ribosomes at codon resolution. Nature 464: 1012-1017.
    • (2010) Nature , vol.464 , pp. 1012-1017
    • Uemura, S.1    Aitken, C.E.2    Korlach, J.3    Flusberg, B.A.4    Turner, S.W.5
  • 12
    • 79955494464 scopus 로고    scopus 로고
    • Single-molecule fluorescence measurements of ribosomal translocation dynamics
    • Chen CL, Stevens B, Kaur J, Cabral D, Liu HQ, et al. (2011) Single-molecule fluorescence measurements of ribosomal translocation dynamics. Mol Cell 42: 367-377.
    • (2011) Mol Cell , vol.42 , pp. 367-377
    • Chen, C.L.1    Stevens, B.2    Kaur, J.3    Cabral, D.4    Liu, H.Q.5
  • 13
    • 80054769463 scopus 로고    scopus 로고
    • Allosteric vs. spontaneous exit-site (E-site) tRNA dissociation early in protein synthesis
    • Chen CL, Stevens B, Kaur J, Smilansky Z, Cooperman BS, et al. (2011) Allosteric vs. spontaneous exit-site (E-site) tRNA dissociation early in protein synthesis. PNAS 108: 16980-16985.
    • (2011) PNAS , vol.108 , pp. 16980-16985
    • Chen, C.L.1    Stevens, B.2    Kaur, J.3    Smilansky, Z.4    Cooperman, B.S.5
  • 14
    • 42949126723 scopus 로고    scopus 로고
    • Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation
    • Fei J, Kosuri P, MacDougall DD, Gonzalez RL, (2008) Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation. Mol Cell 30: 348-359.
    • (2008) Mol Cell , vol.30 , pp. 348-359
    • Fei, J.1    Kosuri, P.2    MacDougall, D.D.3    Gonzalez, R.L.4
  • 15
    • 70349470607 scopus 로고    scopus 로고
    • Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation
    • Fei JY, Bronson JE, Hofman JM, Srinivas RL, Wiggins CH, et al. (2009) Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation. PNAS 106: 15702-15707.
    • (2009) PNAS , vol.106 , pp. 15702-15707
    • Fei, J.Y.1    Bronson, J.E.2    Hofman, J.M.3    Srinivas, R.L.4    Wiggins, C.H.5
  • 16
    • 34548341807 scopus 로고    scopus 로고
    • Fluorescent labeling of tRNAs for dynamics experiments
    • Betteridge T, Liu H, Gamper H, Kirillov S, Cooperman BS, et al. (2007) Fluorescent labeling of tRNAs for dynamics experiments. RNA 13: 1594-1601.
    • (2007) RNA , vol.13 , pp. 1594-1601
    • Betteridge, T.1    Liu, H.2    Gamper, H.3    Kirillov, S.4    Cooperman, B.S.5
  • 17
    • 58249096649 scopus 로고    scopus 로고
    • Synthesis and functional activity of tRNAs labeled with fluorescent hydrazides in the D-loop
    • Pan DL, Qin HO, Cooperman BS, (2009) Synthesis and functional activity of tRNAs labeled with fluorescent hydrazides in the D-loop. RNA 15: 346-354.
    • (2009) RNA , vol.15 , pp. 346-354
    • Pan, D.L.1    Qin, H.O.2    Cooperman, B.S.3
  • 18
    • 0022978468 scopus 로고
    • Allosteric interactions between the ribosomal transfer RNA-Binding Sites A and E
    • Rheinberger HJ, Nierhaus KH, (1986) Allosteric interactions between the ribosomal transfer RNA-Binding Sites A and E. J Biol Chem 261: 9133-9139.
    • (1986) J Biol Chem , vol.261 , pp. 9133-9139
    • Rheinberger, H.J.1    Nierhaus, K.H.2
  • 19
    • 0023000956 scopus 로고
    • Codon-anticodon interaction at the ribosomal-E Site
    • Rheinberger HJ, Sternbach H, Nierhaus KH, (1986) Codon-anticodon interaction at the ribosomal-E Site. J Biol Chem 261: 9140-9143.
    • (1986) J Biol Chem , vol.261 , pp. 9140-9143
    • Rheinberger, H.J.1    Sternbach, H.2    Nierhaus, K.H.3
  • 20
    • 80455168326 scopus 로고    scopus 로고
    • Quantitative single cell monitoring of protein synthesis at subcellular resolution using fluorescently labeled tRNA
    • Barhoom S, Kaur J, Cooperman BS, Smorodinsky NI, Smilansky Z, et al. (2011) Quantitative single cell monitoring of protein synthesis at subcellular resolution using fluorescently labeled tRNA. Nucleic Acids Res 39: e129.
    • (2011) Nucleic Acids Res , vol.39
    • Barhoom, S.1    Kaur, J.2    Cooperman, B.S.3    Smorodinsky, N.I.4    Smilansky, Z.5
  • 22
    • 79960959180 scopus 로고    scopus 로고
    • RNA mimics of green fluorescent protein
    • Paige JS, Wu KY, Jaffrey SR, (2011) RNA mimics of green fluorescent protein. Science 333: 642-646.
    • (2011) Science , vol.333 , pp. 642-646
    • Paige, J.S.1    Wu, K.Y.2    Jaffrey, S.R.3
  • 24
    • 79955506552 scopus 로고    scopus 로고
    • Fluorescent labeling of tRNA dihydrouridine residues: Mechanism and distribution
    • Kaur J, Raj M, Cooperman BS, (2011) Fluorescent labeling of tRNA dihydrouridine residues: Mechanism and distribution. RNA 17: 1393-1400.
    • (2011) RNA , vol.17 , pp. 1393-1400
    • Kaur, J.1    Raj, M.2    Cooperman, B.S.3
  • 25
    • 0018510092 scopus 로고
    • Fluorescent derivatives of yeast transfer RNA-Phe
    • Wintermeyer W, Zachau HG, (1979) Fluorescent derivatives of yeast transfer RNA-Phe. Eur J Biochem 98: 465-475.
    • (1979) Eur J Biochem , vol.98 , pp. 465-475
    • Wintermeyer, W.1    Zachau, H.G.2
  • 26
    • 77954306363 scopus 로고    scopus 로고
    • Site-specific fluorescent probing of RNA molecules by unnatural base-pair transcription for local structural conformation analysis
    • Hikida Y, Kimoto M, Yokoyama S, Hirao I, (2010) Site-specific fluorescent probing of RNA molecules by unnatural base-pair transcription for local structural conformation analysis. Nat Protoc 5: 1312-1323.
    • (2010) Nat Protoc , vol.5 , pp. 1312-1323
    • Hikida, Y.1    Kimoto, M.2    Yokoyama, S.3    Hirao, I.4
  • 27
    • 79953139279 scopus 로고    scopus 로고
    • Expanding the chemical scope of RNA:methyltransferases to site-specific alkynylation of RNA for click labeling
    • Motorin Y, Burhenne J, Teimer R, Koynov K, Willnow S, et al. (2011) Expanding the chemical scope of RNA:methyltransferases to site-specific alkynylation of RNA for click labeling. Nucleic Acids Res 39: 1943-1952.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1943-1952
    • Motorin, Y.1    Burhenne, J.2    Teimer, R.3    Koynov, K.4    Willnow, S.5
  • 28
    • 80052982281 scopus 로고    scopus 로고
    • The dynamic nature of RNA as key to understanding riboswitch mechanisms
    • Haller A, Souliere MF, Micura R, (2011) The dynamic nature of RNA as key to understanding riboswitch mechanisms. Acc Chem Res 12: 1339-1348.
    • (2011) Acc Chem Res , vol.12 , pp. 1339-1348
    • Haller, A.1    Souliere, M.F.2    Micura, R.3
  • 29
    • 0034859439 scopus 로고    scopus 로고
    • Specific polar localization of ribosomes in Bacillus subtilis depends on active transcription
    • Mascarenhas J, Weber MHW, Graumann PL, (2001) Specific polar localization of ribosomes in Bacillus subtilis depends on active transcription. EMBO Rep 2: 685-689.
    • (2001) EMBO Rep , vol.2 , pp. 685-689
    • Mascarenhas, J.1    Weber, M.H.W.2    Graumann, P.L.3
  • 30
    • 0028941626 scopus 로고
    • GTP consumption of elongation-factor Tu during translation of heteropolymeric messenger-RNAs
    • Rodnina MV, Wintermeyer W, (1995) GTP consumption of elongation-factor Tu during translation of heteropolymeric messenger-RNAs. PNAS 92: 1945-1949.
    • (1995) PNAS , vol.92 , pp. 1945-1949
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 31
    • 0019257050 scopus 로고
    • Functional-studies on ribosomes lacking protein L1 from mutant Escherichia-Coli
    • Subramanian AR, Dabbs ER, (1980) Functional-studies on ribosomes lacking protein L1 from mutant Escherichia-Coli. Eur J Biochem 112: 425-430.
    • (1980) Eur J Biochem , vol.112 , pp. 425-430
    • Subramanian, A.R.1    Dabbs, E.R.2
  • 32
    • 66649100512 scopus 로고    scopus 로고
    • Interaction of IF2 with the ribosomal GTPase-associated center during 70S initiation complex formation
    • Qin HO, Grigoriadou C, Cooperman BS, (2009) Interaction of IF2 with the ribosomal GTPase-associated center during 70S initiation complex formation. Biochemistry 48: 4699-4706.
    • (2009) Biochemistry , vol.48 , pp. 4699-4706
    • Qin, H.O.1    Grigoriadou, C.2    Cooperman, B.S.3
  • 33
    • 34648813439 scopus 로고    scopus 로고
    • Single-molecule structural dynamics of EF-G-ribosome interaction during translocation
    • Wang Y, Qin H, Kudaravalli RD, Kirillov SV, Dempsey GT, et al. (2007) Single-molecule structural dynamics of EF-G-ribosome interaction during translocation. Biochemistry 46: 10767-10775.
    • (2007) Biochemistry , vol.46 , pp. 10767-10775
    • Wang, Y.1    Qin, H.2    Kudaravalli, R.D.3    Kirillov, S.V.4    Dempsey, G.T.5
  • 34
    • 16544395270 scopus 로고    scopus 로고
    • Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h
    • Chiu J, March PE, Lee R, Tillett D, (2004) Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h. Nucleic Acids Res 32: e174.
    • (2004) Nucleic Acids Res , vol.32
    • Chiu, J.1    March, P.E.2    Lee, R.3    Tillett, D.4
  • 35
    • 0019274775 scopus 로고
    • Distances between 3′ ends of ribosomal ribonucleic-acids reassembled into Escherichia-Coli ribosomes
    • Odom OW, Robbins DJ, Lynch J, Dottaviomartin D, Kramer G, et al. (1980) Distances between 3′ ends of ribosomal ribonucleic-acids reassembled into Escherichia-Coli ribosomes. Biochemistry 19: 5947-5954.
    • (1980) Biochemistry , vol.19 , pp. 5947-5954
    • Odom, O.W.1    Robbins, D.J.2    Lynch, J.3    Dottaviomartin, D.4    Kramer, G.5
  • 36
    • 2942650138 scopus 로고    scopus 로고
    • Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules
    • Kapanidis AN, Lee NK, Laurence TA, Doose S, Margeat E, et al. (2004) Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules. PNAS 101: 8936-8941.
    • (2004) PNAS , vol.101 , pp. 8936-8941
    • Kapanidis, A.N.1    Lee, N.K.2    Laurence, T.A.3    Doose, S.4    Margeat, E.5
  • 37
    • 0001072895 scopus 로고
    • The use of confidence or fiducial limits illustrated in the case of the binomial
    • Clopper CJ, Pearson ES, (1934) The use of confidence or fiducial limits illustrated in the case of the binomial. Biometrika 26: 404-413.
    • (1934) Biometrika , vol.26 , pp. 404-413
    • Clopper, C.J.1    Pearson, E.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.