메뉴 건너뛰기




Volumn 3, Issue 7, 1997, Pages 748-763

Mutational analysis of the protein subunits of the signal recognition particle Alu-domain

Author keywords

Alu RNA; Dimerization; RNA protein; SRP14; SRP9

Indexed keywords

PROTEIN SUBUNIT;

EID: 0030760923     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (11)

References (53)
  • 1
    • 0028303640 scopus 로고
    • Molecular evolution of SRP cycle components: Functional implications
    • Althoff S, Selinger D, Wise JA. 1994. Molecular evolution of SRP cycle components: Functional implications. Nucleic Acids Res 22:1933-1947.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1933-1947
    • Althoff, S.1    Selinger, D.2    Wise, J.A.3
  • 2
    • 0029963973 scopus 로고    scopus 로고
    • Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
    • Bacher G, Lütcke H, Jungnickel B, Rapoport TA, Dobberstein B. 1996. Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting (see comments). Nature 331:248-251.
    • (1996) Nature , vol.331 , pp. 248-251
    • Bacher, G.1    Lütcke, H.2    Jungnickel, B.3    Rapoport, T.A.4    Dobberstein, B.5
  • 3
    • 0029111710 scopus 로고
    • X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix
    • Biou, V, Shu F, Ramakrishnan V. 1995. X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix. EMBO J 14:4056-4064.
    • (1995) EMBO J , vol.14 , pp. 4056-4064
    • Biou, V.1    Shu, F.2    Ramakrishnan, V.3
  • 4
    • 0030926002 scopus 로고    scopus 로고
    • The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14
    • Forthcoming
    • Birse DEA, Kapp U, Strub K, Cusack S, Åberg A. 1997. The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14. EMBO J. Forthcoming.
    • (1997) EMBO J
    • Birse, D.E.A.1    Kapp, U.2    Strub, K.3    Cusack, S.4    Åberg, A.5
  • 5
    • 0028285681 scopus 로고
    • The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chain
    • Bovia F, Bui N, Strub K. 1994. The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chain. Nucleic Acids Res 22:2028-2035.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2028-2035
    • Bovia, F.1    Bui, N.2    Strub, K.3
  • 6
    • 0029011245 scopus 로고
    • The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs
    • Bovia F, Fornallaz M, Leffers H, Strub K. 1995. The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs. Mol Biol Cell 6:471-484.
    • (1995) Mol Biol Cell , vol.6 , pp. 471-484
    • Bovia, F.1    Fornallaz, M.2    Leffers, H.3    Strub, K.4
  • 7
    • 0029858993 scopus 로고    scopus 로고
    • The signal recognition particle and related small cytoplasmic ribonucleorotein particles
    • Bovia F, Strub K. 1996. The signal recognition particle and related small cytoplasmic ribonucleorotein particles. J Cell Sci 109:2601-2608.
    • (1996) J Cell Sci , vol.109 , pp. 2601-2608
    • Bovia, F.1    Strub, K.2
  • 8
    • 0030862651 scopus 로고    scopus 로고
    • The SRF9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog
    • Bovia F, Wolff N, Ryser S, Strub K. 1997. The SRF9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog. Nucleic Acids Res 25:318-325.
    • (1997) Nucleic Acids Res , vol.25 , pp. 318-325
    • Bovia, F.1    Wolff, N.2    Ryser, S.3    Strub, K.4
  • 9
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D. 1995. NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J 14:3563-3571.
    • (1995) EMBO J , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grunert, S.2    Murzin, A.G.3    Proctor, M.4    St Johnston, D.5
  • 11
    • 0027483055 scopus 로고
    • A cellular protein binds BI and Alu small cytoplasmic RNAs in vitro
    • Chang DY, Maraia RJ. 1993. A cellular protein binds BI and Alu small cytoplasmic RNAs in vitro. J Biol Chem 268:6423-6428.
    • (1993) J Biol Chem , vol.268 , pp. 6423-6428
    • Chang, D.Y.1    Maraia, R.J.2
  • 12
    • 0028302027 scopus 로고
    • A human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNA
    • Chang DY, Nelson B, Bilyeu T, Hsu K, Darlington G, Maraia RJ. 1994. A human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNA. Mol Cell Biol 147:3949-3959.
    • (1994) Mol Cell Biol , vol.147 , pp. 3949-3959
    • Chang, D.Y.1    Nelson, B.2    Bilyeu, T.3    Hsu, K.4    Darlington, G.5    Maraia, R.J.6
  • 13
    • 0030011019 scopus 로고    scopus 로고
    • ser and a seryl-adenylate analogue reveals a conformational switch in the active site
    • ser and a seryl-adenylate analogue reveals a conformational switch in the active site. EMBO J 15:2834-2842.
    • (1996) EMBO J , vol.15 , pp. 2834-2842
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 14
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan GI, Lewis GK, Ramsay G, Bishop JM. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol Cell Biol 5:3610-3616.
    • (1985) Mol Cell Biol , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 15
    • 0028639195 scopus 로고
    • Staufen protein associates with the 3'UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner
    • Ferrandon D, Elphick L, Nusslein-Volhard C, St Johnston D. 1994. Staufen protein associates with the 3'UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner. Cell 79:1221-1232.
    • (1994) Cell , vol.79 , pp. 1221-1232
    • Ferrandon, D.1    Elphick, L.2    Nusslein-Volhard, C.3    St Johnston, D.4
  • 16
    • 0024841329 scopus 로고
    • Saccharomyces cerevisine and Schizosaccharomyces pombe contain a homologue to the 54-kD sub-unit of the signal recognition particle that in S. cerevisiae is essential for growth
    • Hann BC, Poritz MA, Walter P. 1989. Saccharomyces cerevisine and Schizosaccharomyces pombe contain a homologue to the 54-kD sub-unit of the signal recognition particle that in S. cerevisiae is essential for growth. J Cell Biol 109:3223-3230.
    • (1989) J Cell Biol , vol.109 , pp. 3223-3230
    • Hann, B.C.1    Poritz, M.A.2    Walter, P.3
  • 17
    • 0028874760 scopus 로고
    • A complex of the signal sequence binding protein and the SRP RNA promotes transiocation of nascent proteins
    • Hauser S, Bacher G, Dobberstein B, Lutcke H. 1995. A complex of the signal sequence binding protein and the SRP RNA promotes transiocation of nascent proteins. EMBO J 14:5485-5493.
    • (1995) EMBO J , vol.14 , pp. 5485-5493
    • Hauser, S.1    Bacher, G.2    Dobberstein, B.3    Lutcke, H.4
  • 18
    • 0028351855 scopus 로고
    • Nuclear export of signal recognition particle RNA is a facilitated process that involves the Alu sequence domain
    • He XP, Bataille N, Fried HM. 1994. Nuclear export of signal recognition particle RNA is a facilitated process that involves the Alu sequence domain. J Cell Sci 107:903-912.
    • (1994) J Cell Sci , vol.107 , pp. 903-912
    • He, X.P.1    Bataille, N.2    Fried, H.M.3
  • 19
    • 0016153699 scopus 로고
    • Assenbly mapping of 30S ribosomal proteins from Escherichia coli
    • Held WA, Ballou B, Mizushima S, Nomura M. 1974. Assenbly mapping of 30S ribosomal proteins from Escherichia coli. J Biol Chem 249:3103-3111.
    • (1974) J Biol Chem , vol.249 , pp. 3103-3111
    • Held, W.A.1    Ballou, B.2    Mizushima, S.3    Nomura, M.4
  • 20
    • 0026636866 scopus 로고
    • Fluorescence-detected assembly of the signal recognition particle: Binding of the two SRP protein heterodimers to SRP RNA is noncooperative
    • Janiak F, Walter P, Johnson AE. 1992. Fluorescence-detected assembly of the signal recognition particle: Binding of the two SRP protein heterodimers to SRP RNA is noncooperative. Biochemistry 31:5830-5840.
    • (1992) Biochemistry , vol.31 , pp. 5830-5840
    • Janiak, F.1    Walter, P.2    Johnson, A.E.3
  • 21
  • 22
    • 0025981510 scopus 로고
    • SRP-RNA sequence alignment and secondary structure
    • Larsen N, Zwieb C. 1991. SRP-RNA sequence alignment and secondary structure. Nucleic Acids Res 19:209-215.
    • (1991) Nucleic Acids Res , vol.19 , pp. 209-215
    • Larsen, N.1    Zwieb, C.2
  • 24
    • 0028964746 scopus 로고
    • Signal recognition particle (SRP), a ubiquitous initiator of protein translocation
    • Lütcke H. 1995. Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur J Biochem 228:531-550.
    • (1995) Eur J Biochem , vol.228 , pp. 531-550
    • Lütcke, H.1
  • 25
    • 0029030017 scopus 로고
    • Localized bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1
    • Mahone M, Saffman EE, Lasko PF. 1995. Localized bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1. EMBO J 14:2043-2055.
    • (1995) EMBO J , vol.14 , pp. 2043-2055
    • Mahone, M.1    Saffman, E.E.2    Lasko, P.F.3
  • 26
    • 0021770917 scopus 로고
    • Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter
    • Melton DA, Krieg PA, Rebagliati MR, Maniatis T, Zinn K, Green MR 1984. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res 12:7035-7056.
    • (1984) Nucleic Acids Res , vol.12 , pp. 7035-7056
    • Melton, D.A.1    Krieg, P.A.2    Rebagliati, M.R.3    Maniatis, T.4    Zinn, K.5    Green, M.R.6
  • 27
    • 0027433308 scopus 로고
    • GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
    • Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P. 1993. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366:351-354.
    • (1993) Nature , vol.366 , pp. 351-354
    • Miller, J.D.1    Wilhelm, H.2    Gierasch, L.3    Gilmore, R.4    Walter, P.5
  • 28
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan JF, Groebe DR, Witherell GW, Uhlenbeck OC. 1987. Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res 15:8783-8798.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 29
    • 0029988528 scopus 로고    scopus 로고
    • Three-dimensional sturcture and stability of the KH domain: Molecular insights into the fragile X syndrome
    • Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A. 1996. Three-dimensional sturcture and stability of the KH domain: Molecular insights into the fragile X syndrome. Cell 85:237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Castiglione Morelli, M.A.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 30
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai K, Oubridge C, Jessen TH, Li J, Evans PR. 1990. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A [see comments]. Nature 348:515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 31
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge C, Ito N, Evans PR, Teo CH, Nagai K. 1994a. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372:432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 32
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge C, Nobutoshi I, Evans PR, Teo CH, Nagai K. 1994b. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372:432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Nobutoshi, I.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 33
    • 0027404265 scopus 로고
    • The RNA binding site of bacteriophage MS2 coat protein
    • Peabody DS. 1993. The RNA binding site of bacteriophage MS2 coat protein. EMBO J 12:595-600.
    • (1993) EMBO J , vol.12 , pp. 595-600
    • Peabody, D.S.1
  • 34
    • 0029899266 scopus 로고    scopus 로고
    • Complementatoin of RNA binding site mutations in MS2 coat protein heterodimers
    • Peabody DS, Lim F. 1996. Complementatoin of RNA binding site mutations in MS2 coat protein heterodimers. Nucleic Acids Res 24:2352-2359.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2352-2359
    • Peabody, D.S.1    Lim, F.2
  • 35
    • 0026794697 scopus 로고
    • The E. coli ffh gene is necessary for viability and efficient protein transport
    • Phillips GJ, Silhavy TJ. 1992. The E. coli ffh gene is necessary for viability and efficient protein transport. Nature 359:744-746.
    • (1992) Nature , vol.359 , pp. 744-746
    • Phillips, G.J.1    Silhavy, T.J.2
  • 37
    • 0026687213 scopus 로고
    • The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA
    • Ramakrishnan V, White SW. 1992. The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA. Nature 358:768-771.
    • (1992) Nature , vol.358 , pp. 768-771
    • Ramakrishnan, V.1    White, S.W.2
  • 38
    • 0026557511 scopus 로고
    • Protein translocatoin across the ER requires a functional GTP binding site in the α-subunit of the signal recognition particle receptor
    • Rapiejko P, Gilmore R. 1992. Protein translocatoin across the ER requires a functional GTP binding site in the α-subunit of the signal recognition particle receptor. J Cell Biol 117:493-503.
    • (1992) J Cell Biol , vol.117 , pp. 493-503
    • Rapiejko, P.1    Gilmore, R.2
  • 39
    • 0025325983 scopus 로고
    • The megaprimer method of site directed mutagenesis
    • Sarkar G, Sommer SS. 1990. The megaprimer method of site directed mutagenesis. BioTechniques 8:404-407.
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 40
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, Von Jagow G. 1987. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 41
    • 0022620481 scopus 로고
    • Removel of the Alu stuctural domain from signal recognition particle leaves its protein translocation activity intact
    • Siegel V, Walter P. 1986. Removel of the Alu stuctural domain from signal recognition particle leaves its protein translocation activity intact. Nature 320:81-84.
    • (1986) Nature , vol.320 , pp. 81-84
    • Siegel, V.1    Walter, P.2
  • 42
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith DB, Johnson KS. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 43
    • 0025741084 scopus 로고
    • Binding sites of the 9- and 14-kilodalton heterodimetric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution
    • Stub K, Moss J, Walter P. 1991. Binding sites of the 9- and 14-kilodalton heterodimetric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. Mol Cell Biol 11:3949-3959.
    • (1991) Mol Cell Biol , vol.11 , pp. 3949-3959
    • Stub, K.1    Moss, J.2    Walter, P.3
  • 44
    • 0024844289 scopus 로고
    • Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactions
    • Sturb K, Walter P. 1989. Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactions. Proc Natl Acad Sci USA 86:9747-9751.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9747-9751
    • Sturb, K.1    Walter, P.2
  • 45
    • 0025098763 scopus 로고
    • Assembly of the Alu domain of the signal recognition particle (SRP): Dimerization of the two protein components is required for efficiet binding of SRP RNA
    • Strub K, Walter P. 1990. Assembly of the Alu domain of the signal recognition particle (SRP): Dimerization of the two protein components is required for efficiet binding of SRP RNA. Mol Cell Biol 10:777-784.
    • (1990) Mol Cell Biol , vol.10 , pp. 777-784
    • Strub, K.1    Walter, P.2
  • 46
    • 1842272943 scopus 로고
    • The Alu-domain of the signal recognition particle
    • Nierhaus KH, Franceschi F, Subramanian AR, Erdmann VA, Wittmann-Liebold B, ed. New York: Plenum Press
    • Strub K, Wolff N, Oertle S. 1993. The Alu-domain of the signal recognition particle. In: Nierhaus KH, Franceschi F, Subramanian AR, Erdmann VA, Wittmann-Liebold B, ed. The translational apparatus. New York: Plenum Press. pp 635-645.
    • (1993) The Translational Apparatus , pp. 635-645
    • Strub, K.1    Wolff, N.2    Oertle, S.3
  • 48
    • 0021127698 scopus 로고
    • Alu sequences are processed 7SL RNA genes
    • Ulllu E, Tschudi C. 1984. Alu sequences are processed 7SL RNA genes. Nature 312:171-172.
    • (1984) Nature , vol.312 , pp. 171-172
    • Ulllu, E.1    Tschudi, C.2
  • 50
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter P, Johnson AE. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol 10:87-119.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 51
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans
    • Wilson R et al. (1994). 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368:32-38.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1
  • 52
    • 0028365369 scopus 로고
    • From the elephant to E. coli: SRP dependent protein targeting
    • Wolin SL. 1994. From the elephant to E. coli: SRP dependent protein targeting. Cell 77:787-790.
    • (1994) Cell , vol.77 , pp. 787-790
    • Wolin, S.L.1
  • 53
    • 0030342517 scopus 로고    scopus 로고
    • Model of the 3D structure of human SRP RNA
    • Zwieb C, Müller F, Larsen N. 1996. Model of the 3D structure of human SRP RNA. Folding & Design 1:315-324.
    • (1996) Folding & Design , vol.1 , pp. 315-324
    • Zwieb, C.1    Müller, F.2    Larsen, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.