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Volumn 1834, Issue 2, 2013, Pages 559-567

The major mRNP protein YB-1: Structural and association properties in solution

Author keywords

Cold shock domain; Compactness; Disordered protein; Heat and cold denaturation; Oligomerization; Polyproline type II helix

Indexed keywords

COLD SHOCK PROTEIN; OLIGOMER; Y BOX BINDING PROTEIN 1;

EID: 84872116351     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.11.007     Document Type: Article
Times cited : (24)

References (46)
  • 3
    • 33749074121 scopus 로고    scopus 로고
    • Nonspecific and specific interaction of Y-box binding protein 1 (YB-1) with mRNA and posttranscriptional regulation of protein synthesis in animal cells
    • M.A. Skabkin, D.N. Lyabin, and L.P. Ovchinnikov Nonspecific and specific interaction of Y-box binding protein 1 (YB-1) with mRNA and posttranscriptional regulation of protein synthesis in animal cells Mol. Biol. (Mosk) 40 2006 551 563
    • (2006) Mol. Biol. (Mosk) , vol.40 , pp. 551-563
    • Skabkin, M.A.1    Lyabin, D.N.2    Ovchinnikov, L.P.3
  • 4
    • 0026842808 scopus 로고
    • The Y-box factors: A family of nucleic acid binding proteins conserved from Escherichia coli to man
    • A.P. Wolffe, S. Tafuri, M. Ranjan, and M. Familari The Y-box factors: a family of nucleic acid binding proteins conserved from Escherichia coli to man New Biol. 4 1992 290 298
    • (1992) New Biol. , vol.4 , pp. 290-298
    • Wolffe, A.P.1    Tafuri, S.2    Ranjan, M.3    Familari, M.4
  • 5
    • 1842271191 scopus 로고
    • Characterization of the cDNA encoding a protein binding to the major histocompatibility complex class II y box
    • D.K. Didier, J. Schiffenbauer, S.L. Woulfe, M. Zacheis, and B.D. Schwartz Characterization of the cDNA encoding a protein binding to the major histocompatibility complex class II Y box Proc. Natl. Acad. Sci. U. S. A. 85 1988 7322 7326
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 7322-7326
    • Didier, D.K.1    Schiffenbauer, J.2    Woulfe, S.L.3    Zacheis, M.4    Schwartz, B.D.5
  • 7
    • 0032700750 scopus 로고    scopus 로고
    • Interaction of the universal mRNA-binding protein, p50, with actin: A possible link between mRNA and microfilaments
    • P.V. Ruzanov, V.M. Evdokimova, N.L. Korneeva, J.W. Hershey, and L.P. Ovchinnikov Interaction of the universal mRNA-binding protein, p50, with actin: a possible link between mRNA and microfilaments J. Cell Sci. 112 Pt 20 1999 3487 3496
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 20 , pp. 3487-3496
    • Ruzanov, P.V.1    Evdokimova, V.M.2    Korneeva, N.L.3    Hershey, J.W.4    Ovchinnikov, L.P.5
  • 10
    • 0032837139 scopus 로고    scopus 로고
    • Interaction of YB-1 with human immunodeficiency virus type 1 Tat and TAR RNA modulates viral promoter activity
    • S.A. Ansari, M. Safak, G.L. Gallia, B.E. Sawaya, S. Amini, and K. Khalili Interaction of YB-1 with human immunodeficiency virus type 1 Tat and TAR RNA modulates viral promoter activity J. Gen. Virol. 80 Pt 10 1999 2629 2638
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 10 , pp. 2629-2638
    • Ansari, S.A.1    Safak, M.2    Gallia, G.L.3    Sawaya, B.E.4    Amini, S.5    Khalili, K.6
  • 11
    • 0037829212 scopus 로고    scopus 로고
    • The pleiotropic functions of the Y-box-binding protein, YB-1
    • K. Kohno, H. Izumi, T. Uchiumi, M. Ashizuka, and M. Kuwano The pleiotropic functions of the Y-box-binding protein, YB-1 Bioessays 25 2003 691 698
    • (2003) Bioessays , vol.25 , pp. 691-698
    • Kohno, K.1    Izumi, H.2    Uchiumi, T.3    Ashizuka, M.4    Kuwano, M.5
  • 14
  • 15
    • 84860671860 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains
    • S.G. Guryanov, O.M. Selivanova, A.D. Nikulin, G.A. Enin, B.S. Melnik, D.A. Kretov, I.N. Serdyuk, and L.P. Ovchinnikov Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains PLoS One 7 2012 e36969
    • (2012) PLoS One , vol.7 , pp. 36969
    • Guryanov, S.G.1    Selivanova, O.M.2    Nikulin, A.D.3    Enin, G.A.4    Melnik, B.S.5    Kretov, D.A.6    Serdyuk, I.N.7    Ovchinnikov, L.P.8
  • 16
    • 0035368367 scopus 로고    scopus 로고
    • RNA-binding strategies common to cold-shock domain- and RNA recognition motif-containing proteins
    • X. Manival, L. Ghisolfi-Nieto, G. Joseph, P. Bouvet, and M. Erard RNA-binding strategies common to cold-shock domain- and RNA recognition motif-containing proteins Nucleic Acids Res. 29 2001 2223 2233
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2223-2233
    • Manival, X.1    Ghisolfi-Nieto, L.2    Joseph, G.3    Bouvet, P.4    Erard, M.5
  • 18
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • D. Franke, and D.I. Svergun DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering J. Appl. Crystallogr. 42 2009 342 346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 19
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 36 2003 860 864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 21
    • 0033168440 scopus 로고    scopus 로고
    • A thermodynamic study of the 434-repressor N-terminal domain and of its covalently linked dimers
    • J. Ruiz-Sanz, A. Simoncsits, I. Toro, S. Pongor, P.L. Mateo, and V.V. Filimonov A thermodynamic study of the 434-repressor N-terminal domain and of its covalently linked dimers Eur. J. Biochem. 263 1999 246 253
    • (1999) Eur. J. Biochem. , vol.263 , pp. 246-253
    • Ruiz-Sanz, J.1    Simoncsits, A.2    Toro, I.3    Pongor, S.4    Mateo, P.L.5    Filimonov, V.V.6
  • 22
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 24
    • 0021195067 scopus 로고
    • Amino acid, peptide, and protein volume in solution
    • A.A. Zamyatnin Amino acid, peptide, and protein volume in solution Annu. Rev. Biophys. Bioeng. 13 1984 145 165
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1
  • 28
    • 0014378447 scopus 로고
    • Circular dichroism of poly-L-proline in an unordered conformation
    • M.L. Tiffany, and S. Krimm Circular dichroism of poly-L-proline in an unordered conformation Biopolymers 6 1968 1767 1770
    • (1968) Biopolymers , vol.6 , pp. 1767-1770
    • Tiffany, M.L.1    Krimm, S.2
  • 29
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability and function
    • B. Bochicchio, and A.M. Tamburro Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability and function Chirality 14 2002 782 792
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 30
    • 35748941388 scopus 로고    scopus 로고
    • RVCaB, a calcium-binding protein in radish vacuoles, is predominantly an unstructured protein with a polyproline type II helix
    • J. Ishijima, N. Nagasaki, M. Maeshima, and M. Miyano RVCaB, a calcium-binding protein in radish vacuoles, is predominantly an unstructured protein with a polyproline type II helix J. Biochem. 142 2007 201 211
    • (2007) J. Biochem. , vol.142 , pp. 201-211
    • Ishijima, J.1    Nagasaki, N.2    Maeshima, M.3    Miyano, M.4
  • 31
    • 0030809003 scopus 로고    scopus 로고
    • The role of PII conformations in the calculation of peptide fractional helix content
    • S.H. Park, W. Shalongo, and E. Stellwagen The role of PII conformations in the calculation of peptide fractional helix content Protein Sci. 6 1997 1694 1700
    • (1997) Protein Sci. , vol.6 , pp. 1694-1700
    • Park, S.H.1    Shalongo, W.2    Stellwagen, E.3
  • 33
    • 49349102875 scopus 로고    scopus 로고
    • Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state
    • A.L. Cortajarena, G. Lois, E. Sherman, C.S. O'Hern, L. Regan, and G. Haran Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state J. Mol. Biol. 382 2008 203 212
    • (2008) J. Mol. Biol. , vol.382 , pp. 203-212
    • Cortajarena, A.L.1    Lois, G.2    Sherman, E.3    O'Hern, C.S.4    Regan, L.5    Haran, G.6
  • 34
    • 0033997038 scopus 로고    scopus 로고
    • Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA
    • S.A. Petrosian, and G.I. Makhatadze Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA Protein Sci. 9 2000 387 394
    • (2000) Protein Sci. , vol.9 , pp. 387-394
    • Petrosian, S.A.1    Makhatadze, G.I.2
  • 35
    • 0028593677 scopus 로고
    • Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis
    • G.I. Makhatadze, and M.A. Marahiel Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis Protein Sci. 3 1994 2144 2147
    • (1994) Protein Sci. , vol.3 , pp. 2144-2147
    • Makhatadze, G.I.1    Marahiel, M.A.2
  • 36
    • 0025287103 scopus 로고
    • Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects
    • P.L. Privalov, and G.I. Makhatadze Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects J. Mol. Biol. 213 1990 385 391
    • (1990) J. Mol. Biol. , vol.213 , pp. 385-391
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 38
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • D.S. Wishart, B.D. Sykes, and F.M. Richards Relationship between nuclear magnetic resonance chemical shift and protein secondary structure J. Mol. Biol. 222 1991 311 333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 40
    • 0028153795 scopus 로고
    • Planar stacking interactions of arginine and aromatic side-chains in proteins
    • M.M. Flocco, and S.L. Mowbray Planar stacking interactions of arginine and aromatic side-chains in proteins J. Mol. Biol. 235 1994 709 717
    • (1994) J. Mol. Biol. , vol.235 , pp. 709-717
    • Flocco, M.M.1    Mowbray, S.L.2
  • 42
    • 0242639481 scopus 로고    scopus 로고
    • Major core protein p50 of the cytoplasmic mRNP of somatic cells: Expression in Escherichia coli, isolation and partial characterization of the recombinant protein
    • V.A. Ustinov, M.A. Skabkin, D.V. Nashchekin, V.M. Evdokimova, and L.P. Ovchinnikov Major core protein p50 of the cytoplasmic mRNP of somatic cells: expression in Escherichia coli, isolation and partial characterization of the recombinant protein Biochemistry (Mosc) 61 1996 414 419
    • (1996) Biochemistry (Mosc) , vol.61 , pp. 414-419
    • Ustinov, V.A.1    Skabkin, M.A.2    Nashchekin, D.V.3    Evdokimova, V.M.4    Ovchinnikov, L.P.5
  • 43
    • 0037013235 scopus 로고    scopus 로고
    • Positive and negative effects of the major mammalian messenger ribonucleoprotein p50 on binding of 40 S ribosomal subunits to the initiation codon of beta-globin mRNA
    • A.V. Pisarev, M.A. Skabkin, A.A. Thomas, W.C. Merrick, L.P. Ovchinnikov, and I.N. Shatsky Positive and negative effects of the major mammalian messenger ribonucleoprotein p50 on binding of 40 S ribosomal subunits to the initiation codon of beta-globin mRNA J. Biol. Chem. 277 2002 15445 15451
    • (2002) J. Biol. Chem. , vol.277 , pp. 15445-15451
    • Pisarev, A.V.1    Skabkin, M.A.2    Thomas, A.A.3    Merrick, W.C.4    Ovchinnikov, L.P.5    Shatsky, I.N.6
  • 44
    • 48749112645 scopus 로고    scopus 로고
    • Atomic force microscopy reveals binding of mRNA to microtubules mediated by two major mRNP proteins YB-1 and PABP
    • K.G. Chernov, P.A. Curmi, L. Hamon, A. Mechulam, L.P. Ovchinnikov, and D. Pastré Atomic force microscopy reveals binding of mRNA to microtubules mediated by two major mRNP proteins YB-1 and PABP FEBS Lett. 582 2008 2875 2881
    • (2008) FEBS Lett. , vol.582 , pp. 2875-2881
    • Chernov, K.G.1    Curmi, P.A.2    Hamon, L.3    Mechulam, A.4    Ovchinnikov, L.P.5    Pastré, D.6
  • 45
    • 72149114598 scopus 로고    scopus 로고
    • The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G
    • Y. Suzuki, M. Minami, M. Suzuki, K. Abe, S. Zenno, M. Tsujimoto, K. Matsumoto, and Y. Minami The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G J. Biol. Chem. 284 2009 35597 35604
    • (2009) J. Biol. Chem. , vol.284 , pp. 35597-35604
    • Suzuki, Y.1    Minami, M.2    Suzuki, M.3    Abe, K.4    Zenno, S.5    Tsujimoto, M.6    Matsumoto, K.7    Minami, Y.8
  • 46
    • 14044266924 scopus 로고    scopus 로고
    • An acidic protein, YBAP1, mediates the release of YB-1 from mRNA and relieves the translational repression activity of YB-1
    • K. Matsumoto, K.J. Tanaka, and M. Tsujimoto An acidic protein, YBAP1, mediates the release of YB-1 from mRNA and relieves the translational repression activity of YB-1 Mol. Cell. Biol. 25 2005 1779 1792
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1779-1792
    • Matsumoto, K.1    Tanaka, K.J.2    Tsujimoto, M.3


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