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Volumn 43, Issue 29, 2004, Pages 9390-9400

The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RNA;

EID: 3242685090     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036314r     Document Type: Article
Times cited : (18)

References (45)
  • 1
    • 0029839610 scopus 로고    scopus 로고
    • The protein that binds the 3′ end of histone mRNA: A novel RNA-binding protein required for histone pre-mRNA processing
    • Wang, Z. F., Whitfield, M. L., Ingledue, T. C., III, Dominski, Z., and Marzluff, W. F. (1996) The protein that binds the 3′ end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing, Genes Dev. 10, 3028-3040.
    • (1996) Genes Dev. , vol.10 , pp. 3028-3040
    • Wang, Z.F.1    Whitfield, M.L.2    Ingledue III, T.C.3    Dominski, Z.4    Marzluff, W.F.5
  • 2
    • 0031039529 scopus 로고    scopus 로고
    • The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein
    • Martin, F., Schaller, A., Eglite, S., Schumperli, D., and Muller, B. (1997) The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein, EMBO J. 16, 769-778.
    • (1997) EMBO J. , vol.16 , pp. 769-778
    • Martin, F.1    Schaller, A.2    Eglite, S.3    Schumperli, D.4    Muller, B.5
  • 4
    • 0037084461 scopus 로고    scopus 로고
    • The Caenorhabditis elegans histone hairpin-binding protein is required for core histone expression and is essential for embryonic and postembryonic cell division
    • Pettitt, J., Crombie, C., Schumperli, D., and Muller, B. (2002) The Caenorhabditis elegans histone hairpin-binding protein is required for core histone expression and is essential for embryonic and postembryonic cell division, J. Cell Sci. 115, 857-866.
    • (2002) J. Cell Sci. , vol.115 , pp. 857-866
    • Pettitt, J.1    Crombie, C.2    Schumperli, D.3    Muller, B.4
  • 5
    • 0036337468 scopus 로고    scopus 로고
    • The stem-loop binding protein CDL-1 is required for chromosome condensation, progression of cell death and morphogenesis in Caenorhabditis elegans
    • Kodama, Y., Rothman, J. H., Sugimoto, A., and Yamamoto, M. (2002) The stem-loop binding protein CDL-1 is required for chromosome condensation, progression of cell death and morphogenesis in Caenorhabditis elegans, Development 129, 187-196.
    • (2002) Development , vol.129 , pp. 187-196
    • Kodama, Y.1    Rothman, J.H.2    Sugimoto, A.3    Yamamoto, M.4
  • 6
    • 0032931845 scopus 로고    scopus 로고
    • Two Xenopus proteins that bind the 3′ end of histone mRNA: Implications for translational control of histone synthesis during oogenesis
    • Wang, Z. F., Ingledue, T. C., Dominski, Z., Sanchez, R., and Marzluff, W. F. (1999) Two Xenopus proteins that bind the 3′ end of histone mRNA: implications for translational control of histone synthesis during oogenesis, Mol. Cell. Biol. 19, 835-845.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 835-845
    • Wang, Z.F.1    Ingledue, T.C.2    Dominski, Z.3    Sanchez, R.4    Marzluff, W.F.5
  • 7
    • 1342327611 scopus 로고    scopus 로고
    • The sea urchin stem-loop-binding protein: A maternally expressed protein that probably functions in expression of multiple classes of histone mRNA
    • Robertson, A. J., Howard, J. T., Dominski, Z., Schnackenberg, B. J., Sumerel, J. L., McCarthy, J. J., Coffman, J. A., and Marzluff, W. F. (2004) The sea urchin stem-loop-binding protein: a maternally expressed protein that probably functions in expression of multiple classes of histone mRNA, Nucleic Acids Res. 32, 811-818.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 811-818
    • Robertson, A.J.1    Howard, J.T.2    Dominski, Z.3    Schnackenberg, B.J.4    Sumerel, J.L.5    McCarthy, J.J.6    Coffman, J.A.7    Marzluff, W.F.8
  • 8
    • 0036786956 scopus 로고    scopus 로고
    • The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro
    • Sanchez, R., and Marzluff, W. F. (2002) The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro, Mol. Cell. Biol. 22, 7093-7104.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7093-7104
    • Sanchez, R.1    Marzluff, W.F.2
  • 9
    • 0037373095 scopus 로고    scopus 로고
    • Phosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase
    • Zheng, L., Dominski, Z., Yang, X. C., Elms, P., Raska, C. S., Borchers, C. H., and Marzluff, W. F. (2003) Phosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase, Mol. Cell. Biol. 23, 1590-1601.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1590-1601
    • Zheng, L.1    Dominski, Z.2    Yang, X.C.3    Elms, P.4    Raska, C.S.5    Borchers, C.H.6    Marzluff, W.F.7
  • 10
    • 0034128749 scopus 로고    scopus 로고
    • Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms
    • Whitfield, M. L., Zheng, L. X., Baldwin, A., Ohta, T., Hurt, M. M., and Marzluff, W. F. (2000) Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms, Mol. Cell. Biol. 20, 4188-4198.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4188-4198
    • Whitfield, M.L.1    Zheng, L.X.2    Baldwin, A.3    Ohta, T.4    Hurt, M.M.5    Marzluff, W.F.6
  • 11
    • 3242722720 scopus 로고    scopus 로고
    • Ph.D. Thesis, University of North Carolina at Chapel Hill, Chapel Hill, NC
    • Erkmann, J. A. (2003) Ph.D. Thesis, University of North Carolina at Chapel Hill, Chapel Hill, NC.
    • (2003)
    • Erkmann, J.A.1
  • 12
    • 0036898897 scopus 로고    scopus 로고
    • Histone mRNA expression: Multiple levels of cell cycle regulation and important developmental consequences
    • Marzluff, W. F., and Duronio, R. J. (2002) Histone mRNA expression: multiple levels of cell cycle regulation and important developmental consequences, Curr. Opin. Cell Biol. 14, 692-699.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 692-699
    • Marzluff, W.F.1    Duronio, R.J.2
  • 13
    • 0026355522 scopus 로고
    • Regulation of histone mRNA in the unperturbed cell cycle: Evidence suggesting control at two posttranscriptional steps
    • Harris, M. E., Bohni, R., Schneiderman, M. H., Ramamurthy, L., Schumperli, D., and Marzluff, W. F. (1991) Regulation of histone mRNA in the unperturbed cell cycle: evidence suggesting control at two posttranscriptional steps, Mol. Cell. Biol. 11, 2416-2424.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2416-2424
    • Harris, M.E.1    Bohni, R.2    Schneiderman, M.H.3    Ramamurthy, L.4    Schumperli, D.5    Marzluff, W.F.6
  • 14
    • 1542344036 scopus 로고    scopus 로고
    • Drosophila stem-loop binding protein intracellular localization is mediated by phosphorylation and is required for cell cycle-regulated histone mRNA expression
    • Lanzotti, D. J., Kupsco, J. M., Yang, X. C., Dominski, Z., Marzluff, W. F., and Duronio, R. J. (2004) Drosophila stem-loop binding protein intracellular localization is mediated by phosphorylation and is required for cell cycle-regulated histone mRNA expression. Mol. Biol. Cell 15, 1112-1123.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1112-1123
    • Lanzotti, D.J.1    Kupsco, J.M.2    Yang, X.C.3    Dominski, Z.4    Marzluff, W.F.5    Duronio, R.J.6
  • 15
    • 3242687855 scopus 로고    scopus 로고
    • Electrostatic contribution of serine phosphorylation to the Drosophila SLBP-histone mRNA complex
    • Thapar, R., Marzluff, W. F., and Redinbo, M. R. (2004) Electrostatic contribution of serine phosphorylation to the Drosophila SLBP-histone mRNA complex, Biochemistry 43, 9401-9412.
    • (2004) Biochemistry , vol.43 , pp. 9401-9412
    • Thapar, R.1    Marzluff, W.F.2    Redinbo, M.R.3
  • 17
    • 0027569483 scopus 로고
    • Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
    • Grzesiek, S., and Bax, A. (1993) Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins, J. Biomol. NMR 3, 185-204.
    • (1993) J. Biomol. NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 18
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and Kay, L. E. (1994) Gradient-Enhanced Triple-Resonance 3-Dimensional NMR Experiments with Improved Sensitivity, J. Magn. Reson. Ser. B 103, 203-216.
    • (1994) J. Magn. Reson. Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 19
    • 0027568083 scopus 로고
    • A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments
    • Logan, T. M., Olejniczak, E. T., Xu, R. X., and Fesik, S. W. (1993) A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments, J. Biomol. NMR 3, 225-231.
    • (1993) J. Biomol. NMR , vol.3 , pp. 225-231
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 20
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy, Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 21
    • 0026192276 scopus 로고
    • Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with a myosin light chain kinase fragment
    • Spera, S., Ikura, M., and Bax, A. (1991) Measurement of the exchange rates of rapidly exchanging amide protons: application to the study of calmodulin and its complex with a myosin light chain kinase fragment, J. Biomol. NMR 1, 155-165.
    • (1991) J. Biomol. NMR , vol.1 , pp. 155-165
    • Spera, S.1    Ikura, M.2    Bax, A.3
  • 22
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Primary structure effects on peptide group hydrogen exchange, Proteins 17, 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 24
    • 0042029753 scopus 로고    scopus 로고
    • Dipolar waves as NMR maps of helices in proteins
    • Mesleh, M. F., and Opella, S. J. (2003) Dipolar Waves as NMR maps of helices in proteins, J. Magn. Reson. 163, 288-299.
    • (2003) J. Magn. Reson. , vol.163 , pp. 288-299
    • Mesleh, M.F.1    Opella, S.J.2
  • 26
    • 0027731196 scopus 로고
    • Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern
    • Metzler, W. J., Constantine, K. L., Friedrichs, M. S., Bell, A. J., Ernst, E. G., Lavoie, T. B., and Mueller, L. (1993) Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern, Biochemistry 32, 13818-13829.
    • (1993) Biochemistry , vol.32 , pp. 13818-13829
    • Metzler, W.J.1    Constantine, K.L.2    Friedrichs, M.S.3    Bell, A.J.4    Ernst, E.G.5    Lavoie, T.B.6    Mueller, L.7
  • 27
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra, N., and Bax, A. (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium, Science 278, 1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 28
    • 0031851289 scopus 로고    scopus 로고
    • New techniques in structural NMR-anisotropic interactions
    • Prestegard, J. H. (1998) New techniques in structural NMR-anisotropic interactions, Nat. Struct. Biol. 5 (Suppl), 517-522.
    • (1998) Nat. Struct. Biol. , vol.5 , Issue.SUPPL. , pp. 517-522
    • Prestegard, J.H.1
  • 30
    • 0344413866 scopus 로고    scopus 로고
    • Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: Toward the identification of the binding epitope for alpha-dystroglycan
    • Bozzi, M., Bianchi, M., Sciandra, F., Paci, M., Giardina, B., Brancaccio, A., and Cicero, D. O. (2003) Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan, Biochemistry 42, 13717-13724.
    • (2003) Biochemistry , vol.42 , pp. 13717-13724
    • Bozzi, M.1    Bianchi, M.2    Sciandra, F.3    Paci, M.4    Giardina, B.5    Brancaccio, A.6    Cicero, D.O.7
  • 33
    • 0032570318 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations
    • Daughdrill, G. W., Hanely, L. J., and Dahlquist, F. W. (1998) The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations, Biochemistry 37, 1076-1082.
    • (1998) Biochemistry , vol.37 , pp. 1076-1082
    • Daughdrill, G.W.1    Hanely, L.J.2    Dahlquist, F.W.3
  • 34
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and Record, M. T., Jr. (1994) Coupling of local folding to site-specific binding of proteins to DNA, Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 35
    • 0036142684 scopus 로고    scopus 로고
    • A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3′-end processing
    • Dominski, Z., Erkmann, J. A., Yang, X., Sanchez, R., and Marzluff, W. F. (2002) A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3′-end processing, Genes Dev. 16, 58-71.
    • (2002) Genes Dev. , vol.16 , pp. 58-71
    • Dominski, Z.1    Erkmann, J.A.2    Yang, X.3    Sanchez, R.4    Marzluff, W.F.5
  • 36
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm, J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 37
    • 0037099233 scopus 로고    scopus 로고
    • Direct MALDI-MS/MS of phosphopeptides affinity-bound to immobilized metal ion affinity chromatography beads
    • Raska, C. S., Parker, C. E., Dominski, Z., Marzluff, W. F., Glish, G. L., Pope, R. M., and Borchers, C. H. (2002) Direct MALDI-MS/MS of phosphopeptides affinity-bound to immobilized metal ion affinity chromatography beads, Anal. Chem 74, 3429-3433.
    • (2002) Anal. Chem. , vol.74 , pp. 3429-3433
    • Raska, C.S.1    Parker, C.E.2    Dominski, Z.3    Marzluff, W.F.4    Glish, G.L.5    Pope, R.M.6    Borchers, C.H.7
  • 38
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • Dill, K. A., and Shortle, D. (1991) Denatured states of proteins, Annu. Rev. Biochem. 60, 795-825.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 39
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie, J. R., and Shortle, D. (1997) Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures, J. Mol. Biol. 268, 170-184.
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 40
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • Choy, W. Y., and Forman-Kay, J. D. (2001) Calculation of ensembles of structures representing the unfolded state of an SH3 domain, J. Mol. Biol. 308, 1011-1032.
    • (2001) J. Mol. Biol. , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 41
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
    • Dyson, H. J., and Wright, P. E. (2001) Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states, Methods Enzymol. 339, 258-270.
    • (2001) Methods Enzymol. , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 42
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • Shortle, D. R. (1996) Structural analysis of non-native states of proteins by NMR methods, Curr. Opin. Struct. Biol. 6, 24-30.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 43
    • 0036707527 scopus 로고    scopus 로고
    • 3′ end processing of Drosophila melanogaster histone pre-mRNAs: Requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system
    • Dominski, Z., Yang, X. C., Raska, C. S., Santiago, C., Borchers, C. H., Duronio, R. J., and Marzluff, W. F. (2002) 3′ end processing of Drosophila melanogaster histone pre-mRNAs: requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system, Mol. Cell. Biol. 22, 6648-6660.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6648-6660
    • Dominski, Z.1    Yang, X.C.2    Raska, C.S.3    Santiago, C.4    Borchers, C.H.5    Duronio, R.J.6    Marzluff, W.F.7
  • 44
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8M urea
    • Shortle, D., and Ackerman, M. S. (2001) Persistence of native-like topology in a denatured protein in 8M urea, Science 293, 487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 45
    • 0347914553 scopus 로고    scopus 로고
    • Insights into the conformation and dynamics of protein GB 1 during folding and unfolding by NMR
    • Ding, K., Louis, J. M., and Gronenborn, A. M. (2004) Insights into the conformation and dynamics of protein GB 1 during folding and unfolding by NMR, J. Mol. Biol. 335 (5), 1299-1307.
    • (2004) J. Mol. Biol. , vol.335 , Issue.5 , pp. 1299-1307
    • Ding, K.1    Louis, J.M.2    Gronenborn, A.M.3


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