메뉴 건너뛰기




Volumn 337, Issue 2, 2004, Pages 263-272

The location and the significance of a cross-link between the sarcin/ricin domain of ribosomal RNA and the elongation factor-G

Author keywords

EF 2, elongation factor 2; EF G, elongation factor G; EF Tu, elongation factor Tu; Elongation factor G; G domain; GTP hydrolysis; Sarcin ricin domain RNA; SRD, sarcin ricin domain; Translocation; UV, ultraviolet

Indexed keywords

ELONGATION FACTOR G; GUANOSINE TRIPHOSPHATE; IODOURIDINE; OLIGORIBONUCLEOTIDE; PROTEIN; RIBOSOME RNA; RICIN; SARCIN; TRYPTOPHAN; UNCLASSIFIED DRUG; URIDINE DERIVATIVE;

EID: 1442299243     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.01.020     Document Type: Article
Times cited : (12)

References (40)
  • 1
    • 0022319403 scopus 로고
    • Ribosomal translocation: Facts and models
    • Spirin A.S. Ribosomal translocation: facts and models. Prog. Nucl. Acid Res. Mol. Biol. 32:1985;75-114.
    • (1985) Prog. Nucl. Acid Res. Mol. Biol. , vol.32 , pp. 75-114
    • Spirin, A.S.1
  • 4
    • 0030850032 scopus 로고    scopus 로고
    • The conformational properties of elongation factor G and the mechanism of translocation
    • Czworkowski J., Moore P.B. The conformational properties of elongation factor G and the mechanism of translocation. Biochemistry. 36:1997;10327-10334.
    • (1997) Biochemistry , vol.36 , pp. 10327-10334
    • Czworkowski, J.1    Moore, P.B.2
  • 5
    • 0032488946 scopus 로고    scopus 로고
    • Molecular movement inside the translational engine
    • Wilson K.S., Noller H.F. Molecular movement inside the translational engine. Cell. 92:1998;337-349.
    • (1998) Cell , vol.92 , pp. 337-349
    • Wilson, K.S.1    Noller, H.F.2
  • 6
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina M.V., Savelsbergh A., Katunin V.I., Wintermeyer W. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature. 385:1997;37-41.
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 7
    • 0026690643 scopus 로고
    • Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation
    • Wool I.G., Glück A., Endo Y. Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation. Trends Biochem. Sci. 17:1992;266-269.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 266-269
    • Wool, I.G.1    Glück, A.2    Endo, Y.3
  • 8
    • 0028059544 scopus 로고
    • Three-dimensional structure of the ribosomal translocase: Elongation factor G from Thermus thermophilus
    • Ævarsson A., Brazhnikov E., Garber M., Zheltonosova J., Chirgadze Y., al Karadaghi S., et al. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J. 13:1994;3669-3677.
    • (1994) EMBO J. , vol.13 , pp. 3669-3677
    • Ævarsson, A.1    Brazhnikov, E.2    Garber, M.3    Zheltonosova, J.4    Chirgadze, Y.5    Al Karadaghi, S.6
  • 9
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski J., Wang J., Steitz T.A., Moore P.B. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13:1994;3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 10
    • 0030585061 scopus 로고    scopus 로고
    • The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange
    • Al-Karadaghi S., Ævarsson A., Garber M., Zheltonosova J., Liljas A. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure. 4:1996;555-565.
    • (1996) Structure , vol.4 , pp. 555-565
    • Al-Karadaghi, S.1    Ævarsson, A.2    Garber, M.3    Zheltonosova, J.4    Liljas, A.5
  • 11
    • 0025863844 scopus 로고
    • Ribosomal RNA identity elements for ricin A-chain recognition and catalysis
    • Endo Y., Glück A., Wool I.G. Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. J. Mol. Biol. 221:1991;193-207.
    • (1991) J. Mol. Biol. , vol.221 , pp. 193-207
    • Endo, Y.1    Glück, A.2    Wool, I.G.3
  • 12
    • 0001754155 scopus 로고    scopus 로고
    • Structure and mechanism of action of the cytotoxic ribonuclease α-sarcin
    • G. D'Alessio, & J.F. Riordan. San Diego: Academic Press
    • Wool I.G. Structure and mechanism of action of the cytotoxic ribonuclease α-sarcin. D'Alessio G., Riordan J.F. Ribonucleases: Structures and Functions. 1997;131-162 Academic Press, San Diego.
    • (1997) Ribonucleases: Structures and Functions , pp. 131-162
    • Wool, I.G.1
  • 13
    • 0023405923 scopus 로고
    • 2661 region of 23 S rRNA is located at the ribosomal binding sites of both elongation factors
    • 2661 region of 23 S rRNA is located at the ribosomal binding sites of both elongation factors. Biochimie. 69:1987;911-923.
    • (1987) Biochimie , vol.69 , pp. 911-923
    • Hausner, T.P.1    Atmadja, J.2    Nierhaus, K.H.3
  • 14
    • 0030774277 scopus 로고    scopus 로고
    • The ribosome-in-pieces: Binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23 S ribosomal RNA
    • Munishkin A., Wool I.G. The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23 S ribosomal RNA. Proc. Natl Acad. Sci. USA. 94:1997;12280-12284.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12280-12284
    • Munishkin, A.1    Wool, I.G.2
  • 15
    • 0013872227 scopus 로고
    • Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system
    • Nishizuka Y., Lipmann F. Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system. Proc. Natl Acad. Sci. USA. 55:1966;212-219.
    • (1966) Proc. Natl Acad. Sci. USA , vol.55 , pp. 212-219
    • Nishizuka, Y.1    Lipmann, F.2
  • 16
    • 0019889508 scopus 로고
    • Properties and regulation of the GTPase activities of elongation factors Tu and G and of initiation factor 2
    • Parmeggiani A., Sander G. Properties and regulation of the GTPase activities of elongation factors Tu and G and of initiation factor 2. Mol. Cell. Biochem. 35:1981;129-158.
    • (1981) Mol. Cell. Biochem. , vol.35 , pp. 129-158
    • Parmeggiani, A.1    Sander, G.2
  • 17
    • 0032498266 scopus 로고    scopus 로고
    • Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing
    • Wilson K.S., Noller H.F. Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing. Cell. 92:1998;131-139.
    • (1998) Cell , vol.92 , pp. 131-139
    • Wilson, K.S.1    Noller, H.F.2
  • 18
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of elongation factor G on the Escherichia coli 70 S ribosome: The mechanism of translocation
    • Agrawal R.K., Penczek P., Grassucci R.A., Frank J. Visualization of elongation factor G on the Escherichia coli 70 S ribosome: the mechanism of translocation. Proc. Natl Acad. Sci. USA. 95:1998;6134-6138.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6134-6138
    • Agrawal, R.K.1    Penczek, P.2    Grassucci, R.A.3    Frank, J.4
  • 20
    • 0033863336 scopus 로고    scopus 로고
    • Domain motions of EF-G bound to the 70 S ribosome: Insights from a hand-shaking between multi-resolution structures
    • Wriggers W., Agrawal R.K., Drew D.L., McCammon A., Frank J. Domain motions of EF-G bound to the 70 S ribosome: insights from a hand-shaking between multi-resolution structures. Biophys. J. 79:2000;1670-1678.
    • (2000) Biophys. J. , vol.79 , pp. 1670-1678
    • Wriggers, W.1    Agrawal, R.K.2    Drew, D.L.3    McCammon, A.4    Frank, J.5
  • 21
    • 0033578939 scopus 로고    scopus 로고
    • The two faces of the 23 S rRNA sarcin/ricin domain: The structure at 1. 11 Å
    • Correll C.C., Wool I.G., Munishkin A. The two faces of the 23 S rRNA sarcin/ricin domain: the structure at 1.11 Å J. Mol. Biol. 292:1999;275-287.
    • (1999) J. Mol. Biol. , vol.292 , pp. 275-287
    • Correll, C.C.1    Wool, I.G.2    Munishkin, A.3
  • 22
    • 0033593240 scopus 로고    scopus 로고
    • The phenotype of mutations of G2655 in the sarcin/ricin domain of 23 S ribosomal RNA
    • Macbeth M.R., Wool I.G. The phenotype of mutations of G2655 in the sarcin/ricin domain of 23 S ribosomal RNA. J. Mol. Biol. 285:1999;965-975.
    • (1999) J. Mol. Biol. , vol.285 , pp. 965-975
    • MacBeth, M.R.1    Wool, I.G.2
  • 23
    • 0027717964 scopus 로고
    • Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins
    • Willis M.C., Hicke B.J., Uhlenbeck O.C., Cech T.R., Koch T.H. Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins. Science. 262:1993;1255-1257.
    • (1993) Science , vol.262 , pp. 1255-1257
    • Willis, M.C.1    Hicke, B.J.2    Uhlenbeck, O.C.3    Cech, T.R.4    Koch, T.H.5
  • 24
    • 53249132910 scopus 로고    scopus 로고
    • Contact sites of peptide-oligoribonucleotide cross-links identified by a combination of peptide and nucleotide sequencing with MALDI MS
    • Urlaub H., Thiede B., Muller E.C., Wittmann-Liebold B. Contact sites of peptide-oligoribonucleotide cross-links identified by a combination of peptide and nucleotide sequencing with MALDI MS. J. Protein Chem. 16:1997;375-383.
    • (1997) J. Protein Chem. , vol.16 , pp. 375-383
    • Urlaub, H.1    Thiede, B.2    Muller, E.C.3    Wittmann-Liebold, B.4
  • 25
    • 0034685615 scopus 로고    scopus 로고
    • The phenotype of mutations of the base pair C2658·G2663 that closes the tetraloop in the sarcin/ricin domain of Escherichia coli 23 S ribosomal RNA
    • Chan Y.L., Sitikov A.S., Wool I.G. The phenotype of mutations of the base pair C2658·G2663 that closes the tetraloop in the sarcin/ricin domain of Escherichia coli 23 S ribosomal RNA. J. Mol. Biol. 298:2000;795-805.
    • (2000) J. Mol. Biol. , vol.298 , pp. 795-805
    • Chan, Y.L.1    Sitikov, A.S.2    Wool, I.G.3
  • 27
    • 0028214276 scopus 로고
    • Fusidic acid-resistant mutants define three regions in elongation factor G of Salmonella typhimurium
    • Johanson U., Hughes D. Fusidic acid-resistant mutants define three regions in elongation factor G of Salmonella typhimurium. Gene. 143:1994;55-59.
    • (1994) Gene , vol.143 , pp. 55-59
    • Johanson, U.1    Hughes, D.2
  • 28
    • 0015962113 scopus 로고
    • A resolution of conflicting reports concerning the mode of action of fusidic acid
    • Burns K., Cannon M., Cundliffe E. A resolution of conflicting reports concerning the mode of action of fusidic acid. FEBS Letters. 40:1974;219-223.
    • (1974) FEBS Letters , vol.40 , pp. 219-223
    • Burns, K.1    Cannon, M.2    Cundliffe, E.3
  • 29
    • 0016737059 scopus 로고
    • Some characteristics of and structural requirements for the interaction of 24,25-dihydrofusidic acid with ribosome - Elongation factor G complexes
    • Willie G.R., Richman N., Godtfredsen W.P., Bodley J.W. Some characteristics of and structural requirements for the interaction of 24,25-dihydrofusidic acid with ribosome - elongation factor G complexes. Biochemistry. 14:1975;1713-1718.
    • (1975) Biochemistry , vol.14 , pp. 1713-1718
    • Willie, G.R.1    Richman, N.2    Godtfredsen, W.P.3    Bodley, J.W.4
  • 31
    • 0028238349 scopus 로고
    • Elongation factor Tu: A regulatory GTPase with an integrated effector
    • Sprinzl M. Elongation factor Tu: a regulatory GTPase with an integrated effector. Trends Biochem. Sci. 19:1994;245-250.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 245-250
    • Sprinzl, M.1
  • 32
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 349:1991;117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 34
    • 0034603196 scopus 로고    scopus 로고
    • Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
    • Stark H., Rodnina M.V., Wieden H.-J., van Heel M., Wintermeyer W. Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell. 100:2000;301-309.
    • (2000) Cell , vol.100 , pp. 301-309
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.-J.3    Van Heel, M.4    Wintermeyer, W.5
  • 35
    • 0032982866 scopus 로고    scopus 로고
    • EF-G dependent GTP hydrolysis induces translocation accompanied by large conformation changes in the 70 S ribosome
    • Agrawal R.K., Heagle A.B., Penczek P., Grassucci R.A., Frank J. EF-G dependent GTP hydrolysis induces translocation accompanied by large conformation changes in the 70 S ribosome. Nature Struct. Biol. 6:1999;643-647.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 37
    • 0023917453 scopus 로고
    • The cytotoxins alpha-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28 S ribosomal ribonucleic acid
    • Endo Y., Chan Y.L., Lin A., Tsurugi K., Wool I.G. The cytotoxins alpha-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28 S ribosomal ribonucleic acid. J. Biol. Chem. 263:1988;7917-7920.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7917-7920
    • Endo, Y.1    Chan, Y.L.2    Lin, A.3    Tsurugi, K.4    Wool, I.G.5
  • 39
    • 12444276102 scopus 로고
    • Crosslinking of an iodo-uridine-RNA hairpin to a single site on the human U1A N-terminal RNA binding domain
    • Stump W.T., Hall K. Crosslinking of an iodo-uridine-RNA hairpin to a single site on the human U1A N-terminal RNA binding domain. RNA. 1:1995;55-63.
    • (1995) RNA , vol.1 , pp. 55-63
    • Stump, W.T.1    Hall, K.2
  • 40
    • 0018338493 scopus 로고
    • Isolation of physically and enzymically homogeneous Escherichia coli elongation factor G
    • Rohrbach M.S., Bodley J.W. Isolation of physically and enzymically homogeneous Escherichia coli elongation factor G. Methods Enzymol. 60:1979;606-614.
    • (1979) Methods Enzymol. , vol.60 , pp. 606-614
    • Rohrbach, M.S.1    Bodley, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.