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Empty site forms of the SRP54 and SRα GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum
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Rapiejko, P.J.1
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Connolly T., Gilmore R. The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide. Cell. 57:1989;599-610.
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Miller J.D., Wilhelm H., Gierasch L., Gilmore R., Walter P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature. 366:1993;351-354.
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Powers, T.1
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The ribosome regulates the GTPase of the β-subunit of the signal recognition particle receptor
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Bacher G., Pool M., Dobberstein B. The ribosome regulates the GTPase of the β-subunit of the signal recognition particle receptor. J. Cell Biol. 146:1999;723-730.
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SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon
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Fulga T.A., Sinning I., Dobberstein B., Pool M.R. SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon. EMBO J. 20:2001;2338-2347.
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13
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0037162838
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Distinct modes of signal recognition particle interaction with the ribosome
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The authors present data from cross-linking studies that support the idea that SRP54 binds directly to the ribosomal proteins L23a and L35. The environment of SRP54 is studied during defined stages of targeting, which provides a mechanism for receptor interaction at the ribosome.
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Pool M.R., Stumm J., Fulga T.A., Sinning I., Dobberstein B. Distinct modes of signal recognition particle interaction with the ribosome. Science. 297:2002;1345-1348 The authors present data from cross-linking studies that support the idea that SRP54 binds directly to the ribosomal proteins L23a and L35. The environment of SRP54 is studied during defined stages of targeting, which provides a mechanism for receptor interaction at the ribosome.
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Science
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Pool, M.R.1
Stumm, J.2
Fulga, T.A.3
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The signal recognition particle of Archaea
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Eichler J., Moll R. The signal recognition particle of Archaea. Trends Microbiol. 9:2001;130-136.
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A highly recommended review on the assembly and function of archaeal SRP.
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Zwieb C., Eichler J. Getting on target: the archaeal signal recognition particle. Archaea. 1:2002;27-34 A highly recommended review on the assembly and function of archaeal SRP.
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Archaea
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Zwieb, C.1
Eichler, J.2
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0025605808
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An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle
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Poritz M.A., Bernstein H.D., Strub K., Zopf D., Wilhelm H., Walter P. An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science. 250:1990;1111-1117.
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Poritz, M.A.1
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Walter, P.6
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18
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0025009469
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E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle
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Ribes V., Romisch K., Giner A., Dobberstein B., Tollervey D. E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle. Cell. 63:1990;591-600.
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Ribes, V.1
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The N-domain of the signal recognition particle 54-kDa subunit promotes efficient signal sequence binding
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Newitt J.A., Bernstein H.D. The N-domain of the signal recognition particle 54-kDa subunit promotes efficient signal sequence binding. Eur. J. Biochem. 245:1997;720-729.
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Newitt, J.A.1
Bernstein, H.D.2
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20
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0034681490
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Crystal structure of the ribonucleoprotein core of the signal recognition particle
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Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A. Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science. 287:2000;1232-1239.
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Batey, R.T.1
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0035896023
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Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle
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Batey R.T., Sagar M.B., Doudna J.A. Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle. J. Mol. Biol. 307:2001;229-246.
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0034596007
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Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor
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Peluso P., Herschlag D., Nock S., Freymann D.M., Johnson A.E., Walter P. Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor. Science. 288:2000;1640-1643.
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Peluso, P.1
Herschlag, D.2
Nock, S.3
Freymann, D.M.4
Johnson, A.E.5
Walter, P.6
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23
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0035909810
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Role of SRP RNA in the GTPase cycles of Ffh and FtsY
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This detailed kinetic and thermodynamic study provides rate and equilibrium constants for the individual GTP-driven reaction steps that occur on interaction of Ffh and FtsY. The data suggest that 4.5S RNA has an important catalytic function and accelerates the association of Ffh and FtsY in their GTP-bound form.
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Peluso P., Shan S.O., Nock S., Herschlag D., Walter P. Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry. 40:2001;15224-15233 This detailed kinetic and thermodynamic study provides rate and equilibrium constants for the individual GTP-driven reaction steps that occur on interaction of Ffh and FtsY. The data suggest that 4.5S RNA has an important catalytic function and accelerates the association of Ffh and FtsY in their GTP-bound form.
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Biochemistry
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Peluso, P.1
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24
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0035256512
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Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY
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Jagath J.R., Matassova N.B., de Leeuw E., Warnecke J.M., Lentzen G., Rodnina M.V., Luirink J., Wintermeyer W. Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY. RNA. 7:2001;293-301.
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Jagath, J.R.1
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Disassembly and reconstitution of signal recognition particle
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27
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0034602645
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Politz J.C., Yarovoi S., Kilroy S.M., Gowda K., Zwieb C., Pederson T. Signal recognition particle components in the nucleolus. Proc. Natl. Acad. Sci. U.S.A. 97:2000;55-60.
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28
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0033556288
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Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens Ffh-homologous protein suggest an SRP-like complex in archaea
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Moll R., Schmidtke S., Schafer G. Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens Ffh-homologous protein suggest an SRP-like complex in archaea. Eur. J. Biochem. 259:1999;441-448.
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Bhuiyan S.H., Gowda K., Hotokezaka H., Zwieb C. Assembly of archaeal signal recognition particle from recombinant components. Nucleic Acids Res. 28:2000;1365-1373.
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Bhuiyan, S.H.1
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Zwieb, C.4
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30
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0035798197
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An archaeal protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA
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These authors describe the purification and assembly of SRP54 and SRP RNA from the hyperthermophilic archaeon Pyrococcus furiosus. In agreement with similar studies on other archaeal species, the data show that SRP54 can bind to SRP RNA without the presence of SRP19.
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Maeshima H., Okuno E., Aimi T., Morinaga T., Itoh T. An archaeal protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA. FEBS Lett. 507:2001;336-340 These authors describe the purification and assembly of SRP54 and SRP RNA from the hyperthermophilic archaeon Pyrococcus furiosus. In agreement with similar studies on other archaeal species, the data show that SRP54 can bind to SRP RNA without the presence of SRP19.
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FEBS Lett.
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Maeshima, H.1
Okuno, E.2
Aimi, T.3
Morinaga, T.4
Itoh, T.5
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31
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0036799450
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Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii
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The authors describe the purification and reconstitution of SRP19, SRP54 and SRP RNA from the halophilic archaeon Haloferax volcanii. The data show that SRP54 can bind to SRP RNA without the presence of SRP19. A noticeable difference in the S-domain assembly, as compared with other archaeal species, is that SRP54 binding seems to enhance the binding of SRP19. It is speculated that this could be due to direct contacts formed between the proteins when bound to SRP RNA.
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Tozik I., Huang Q., Zwieb C., Eichler J. Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii. Nucleic Acids Res. 30:2002;4166-4175 The authors describe the purification and reconstitution of SRP19, SRP54 and SRP RNA from the halophilic archaeon Haloferax volcanii. The data show that SRP54 can bind to SRP RNA without the presence of SRP19. A noticeable difference in the S-domain assembly, as compared with other archaeal species, is that SRP54 binding seems to enhance the binding of SRP19. It is speculated that this could be due to direct contacts formed between the proteins when bound to SRP RNA.
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Nucleic Acids Res.
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Tozik, I.1
Huang, Q.2
Zwieb, C.3
Eichler, J.4
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32
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0034711041
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Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle
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Diener J.L., Wilson C. Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle. Biochemistry. 39:2000;12862-12874.
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Biochemistry
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Diener, J.L.1
Wilson, C.2
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0035007334
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Visualizing induced fit in early assembly of the human signal recognition particle
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Rose M.A., Weeks K.M. Visualizing induced fit in early assembly of the human signal recognition particle. Nat. Struct. Biol. 8:2001;515-520.
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Rose, M.A.1
Weeks, K.M.2
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35
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Wild K., Weichenrieder O., Strub K., Sinning I., Cusack S. Towards the structure of the mammalian signal recognition particle. Curr. Opin. Struct. Biol. 12:2002;72-81.
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Wild, K.1
Weichenrieder, O.2
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Sinning, I.4
Cusack, S.5
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36
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0037071839
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Structure of the SRP19 RNA complex and implications for signal recognition particle assembly
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Crystal structure of the binary complex of SRP19 and the S domain of 7S RNA from the archaeon Methanococcus jannaschii. This 2.3 Å structure reveals the molecular basis for SRP19 binding to the S domain and describes the RNA-RNA interactions that form in the archaeal S domain. Nucleotides in the asymmetric loop are looped out and surface exposed. Two adenosines from helix 6 make contact with the RNA backbone of helix 8 and stabilise the conformation of the asymmetric loop. The structure provides a mechanism for S-domain assembly in archaea.
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Hainzl T., Huang S., Sauer-Eriksson A.E. Structure of the SRP19 RNA complex and implications for signal recognition particle assembly. Nature. 417:2002;767-771 Crystal structure of the binary complex of SRP19 and the S domain of 7S RNA from the archaeon Methanococcus jannaschii. This 2.3 Å structure reveals the molecular basis for SRP19 binding to the S domain and describes the RNA-RNA interactions that form in the archaeal S domain. Nucleotides in the asymmetric loop are looped out and surface exposed. Two adenosines from helix 6 make contact with the RNA backbone of helix 8 and stabilise the conformation of the asymmetric loop. The structure provides a mechanism for S-domain assembly in archaea.
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(2002)
Nature
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Hainzl, T.1
Huang, S.2
Sauer-Eriksson, A.E.3
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37
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0036289536
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Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle
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This paper describes the 2.9 Å crystal structure of the noncognate complex between SRP19 from M. jannaschii and human S domain. The nucleotides situated in the asymmetric loop have their bases directed towards the centre of the helical axis and are stacked discontinuously.
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Oubridge C., Kuglstatter A., Jovine L., Nagai K. Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle. Mol. Cell. 9:2002;1251-1261 This paper describes the 2.9 Å crystal structure of the noncognate complex between SRP19 from M. jannaschii and human S domain. The nucleotides situated in the asymmetric loop have their bases directed towards the centre of the helical axis and are stacked discontinuously.
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(2002)
Mol. Cell
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Oubridge, C.1
Kuglstatter, A.2
Jovine, L.3
Nagai, K.4
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38
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0036785939
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Induced structural changes of 7SL RNA during the assembly of human signal recognition particle
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This paper describes the 3.1 Å crystal structure of the ternary complex of human SRP19, SRP54 (M domain) and the S domain of 7SL RNA. Binding of the M domain induces a collapse of the asymmetric loop in the S domain. Two adenine bases situated in the short strand flip out and form an A-minor motif with helix 6. A mechanism for the S-domain assembly in human is presented.
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Kuglstatter A., Oubridge C., Nagai K. Induced structural changes of 7SL RNA during the assembly of human signal recognition particle. Nat. Struct. Biol. 9:2002;740-744 This paper describes the 3.1 Å crystal structure of the ternary complex of human SRP19, SRP54 (M domain) and the S domain of 7SL RNA. Binding of the M domain induces a collapse of the asymmetric loop in the S domain. Two adenine bases situated in the short strand flip out and form an A-minor motif with helix 6. A mechanism for the S-domain assembly in human is presented.
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Nat. Struct. Biol.
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Kuglstatter, A.1
Oubridge, C.2
Nagai, K.3
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39
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0032709518
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Structure of the phylogenetically most conserved domain of SRP RNA
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Schmitz U., Behrens S., Freymann D.M., Keenan R.J., Lukavsky P., Walter P., James T.L. Structure of the phylogenetically most conserved domain of SRP RNA. RNA. 5:1999;1419-1429.
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RNA
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Schmitz, U.1
Behrens, S.2
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Keenan, R.J.4
Lukavsky, P.5
Walter, P.6
James, T.L.7
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40
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0034657954
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Crystal structure of the Ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA
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Jovine L., Hainzl T., Oubridge C., Scott W.G., Li J., Sixma T.K., Wonacott A., Skarzynski T., Nagai K. Crystal structure of the Ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA. Struct. Fold Des. 8:2000;527-540.
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Struct. Fold Des.
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Jovine, L.1
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Oubridge, C.3
Scott, W.G.4
Li, J.5
Sixma, T.K.6
Wonacott, A.7
Skarzynski, T.8
Nagai, K.9
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41
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0035913989
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Crystal structure of an early protein-RNA assembly complex of the signal recognition particle
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Wild K., Sinning I., Cusack S. Crystal structure of an early protein-RNA assembly complex of the signal recognition particle. Science. 294:2001;598-601.
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Science
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Wild, K.1
Sinning, I.2
Cusack, S.3
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42
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0036290864
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Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle
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This paper describes the NMR-derived structure of SRP19 from Archaeoglobus fulgidus. The structure is similar to structures of SRP19 determined in complex with SRP RNA, which suggests that SRP19 binds to RNA as a rigid molecule.
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Pakhomova O.N., Deep S., Huang Q., Zwieb C., Hinck A.P. Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle. J. Mol. Biol. 317:2002;145-158 This paper describes the NMR-derived structure of SRP19 from Archaeoglobus fulgidus. The structure is similar to structures of SRP19 determined in complex with SRP RNA, which suggests that SRP19 binds to RNA as a rigid molecule.
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J. Mol. Biol.
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Pakhomova, O.N.1
Deep, S.2
Huang, Q.3
Zwieb, C.4
Hinck, A.P.5
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43
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0026694666
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Recognition of a tetranucleotide loop of signal recognition particle RNA by protein SRP19
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Zwieb C. Recognition of a tetranucleotide loop of signal recognition particle RNA by protein SRP19. J. Biol. Chem. 267:1992;15650-15656.
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Zwieb, C.1
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0028300845
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Site-directed mutagenesis of signal-recognition particle RNA. Identification of the nucleotides in helix 8 required for interaction with protein SRP19
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Zwieb C. Site-directed mutagenesis of signal-recognition particle RNA. Identification of the nucleotides in helix 8 required for interaction with protein SRP19. Eur. J. Biochem. 222:1994;885-890.
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