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Volumn 10, Issue 7, 2003, Pages 545-552

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

Author keywords

[No Author keywords available]

Indexed keywords

EPSILON N METHYLLYSINE; HISTONE H3; HISTONE H4; HOLOENZYME; LARGE SUBUNIT METHYLTRANSFERASE; LYSINE; LYSINE DERIVATIVE; METHYL GROUP; PROTEIN; PROTEIN METHYLTRANSFERASE; RIBULOSEBISPHOSPHATE CARBOXYLASE; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; SET DOMAIN PROTEIN; UNCLASSIFIED DRUG;

EID: 0038419637     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb946     Document Type: Article
Times cited : (114)

References (48)
  • 1
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides, T. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12, 198-209 (2002).
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 2
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M. & Jenuwein, T. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14, 286-298 (2002).
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 3
    • 0035370439 scopus 로고    scopus 로고
    • Histone methylation versus histone acetylation: New insights into epigenetic regulation
    • Rice, J.C. & Allis, C.D. Histone methylation versus histone acetylation: new insights into epigenetic regulation. Curr. Opin. Cell Biol. 13, 263-273 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 263-273
    • Rice, J.C.1    Allis, C.D.2
  • 4
    • 0033592999 scopus 로고    scopus 로고
    • Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena
    • Strahl, B.D., Ohba, R., Cook, R.G. & Allis, C.D. Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena. Proc. Natl. Acad. Sci. USA 96, 14967-14972 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14967-14972
    • Strahl, B.D.1    Ohba, R.2    Cook, R.G.3    Allis, C.D.4
  • 5
    • 0035839110 scopus 로고    scopus 로고
    • Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries
    • Noma, K., Allis, C.D. & Grewal, S.I. Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries. Science 293, 1150-1155 (2001).
    • (2001) Science , vol.293 , pp. 1150-1155
    • Noma, K.1    Allis, C.D.2    Grewal, S.I.3
  • 6
    • 0024636180 scopus 로고
    • Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase
    • Houtz, R.L., Stults, J.T., Mulligan, R.M. & Tolbert, N.E. Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase. Proc. Natl. Acad. Sci. USA 86, 1855-1859 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1855-1859
    • Houtz, R.L.1    Stults, J.T.2    Mulligan, R.M.3    Tolbert, N.E.4
  • 7
    • 0029169542 scopus 로고
    • Cloning and developmental expression of pea ribulose-1,5bisphosphate carboxylase/oxygenase large subunit N-methyltransferase
    • Klein, R.R. & Houtz, R.L. Cloning and developmental expression of pea ribulose-1,5bisphosphate carboxylase/oxygenase large subunit N-methyltransferase. Plant Mol. Biol. 27, 249-261 (1995).
    • (1995) Plant Mol. Biol. , vol.27 , pp. 249-261
    • Klein, R.R.1    Houtz, R.L.2
  • 8
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P. & Ponting, C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA 95, 5857-5864 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 9
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H 3 methyltransferases
    • Rea, S. et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406, 593-599 (2000).
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 10
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410, 116-120 (2001).
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 11
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • Bannister, A.J. et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410, 120-124 (2001).
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1
  • 12
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • Nakayama, J., Rice, J.C., Strahl, B.D., Allis, C.D. & Grewal, S.I. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110-113 (2001).
    • (2001) Science , vol.292 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.5
  • 13
    • 0037172993 scopus 로고    scopus 로고
    • Methylation of histone H3 Lys 4 in coding regions of active genes
    • Bernstein, B.E. et al. Methylation of histone H3 Lys 4 in coding regions of active genes. Proc. Natl. Acad. Sci. USA 99, 8695-8700 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8695-8700
    • Bernstein, B.E.1
  • 14
    • 0037179716 scopus 로고    scopus 로고
    • Active genes are tri-methylated at K4 of histone H3
    • Santos-Rosa, H. et al. Active genes are tri-methylated at K4 of histone H3. Nature 419, 407-411 (2002).
    • (2002) Nature , vol.419 , pp. 407-411
    • Santos-Rosa, H.1
  • 15
    • 0037020217 scopus 로고    scopus 로고
    • Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase
    • Zhang, X. et al. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell 111, 117-127 (2002).
    • (2002) Cell , vol.111 , pp. 117-127
    • Zhang, X.1
  • 16
    • 0036829013 scopus 로고    scopus 로고
    • The active site of the SET domain is constructed on a knot
    • Jacobs, S.A. et al. The active site of the SET domain is constructed on a knot. Nat. Struct. Biol. 9, 833-838 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 833-838
    • Jacobs, S.A.1
  • 17
    • 0037439085 scopus 로고    scopus 로고
    • Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet
    • Kwon, T. et al. Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J. 22, 292-303 (2003).
    • (2003) EMBO J. , vol.22 , pp. 292-303
    • Kwon, T.1
  • 18
    • 0037020032 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the histone methyltransferase SET7/9
    • Wilson, J.R. et al. Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell 111, 105-115 (2002).
    • (2002) Cell , vol.111 , pp. 105-115
    • Wilson, J.R.1
  • 19
    • 0037421847 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the human histone methyltransferase SET7/9
    • Xiao, B. et al. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 421, 652-656 (2003).
    • (2003) Nature , vol.421 , pp. 652-656
    • Xiao, B.1
  • 20
    • 0036829968 scopus 로고    scopus 로고
    • Structure of the SET domain histone lysine methyltransferase Clr4
    • Min, J., Zhang, X., Cheng, X., Grewal, S.I. & Xu, R.M. Structure of the SET domain histone lysine methyltransferase Clr4. Nat. Struct. Biol. 9, 828-832 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 828-832
    • Min, J.1    Zhang, X.2    Cheng, X.3    Grewal, S.I.4    Xu, R.M.5
  • 21
    • 0037337003 scopus 로고    scopus 로고
    • A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3
    • Manzur, K.L. et al. A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3. Nat. Struct. Biol. 10, 187-196 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 187-196
    • Manzur, K.L.1
  • 22
    • 0037020199 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of a SET domain protein methyltransferase
    • Trievel, R.C., Beach, B.M., Dirk, L.M., Houtz, R.L. & Hurley, J.H. Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell 111, 91-103 (2002).
    • (2002) Cell , vol.111 , pp. 91-103
    • Trievel, R.C.1    Beach, B.M.2    Dirk, L.M.3    Houtz, R.L.4    Hurley, J.H.5
  • 23
    • 0037309997 scopus 로고    scopus 로고
    • Structure of SET domain proteins: A new twist on histone methylation
    • Marmorstein, R. Structure of SET domain proteins: a new twist on histone methylation. Trends Biochem. Sci. 28, 59-62 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 59-62
    • Marmorstein, R.1
  • 24
    • 0037020195 scopus 로고    scopus 로고
    • Structures of SET domain proteins: Protein lysine methyltransferases make their mark
    • Yeates, T.O. Structures of SET domain proteins: protein lysine methyltransferases make their mark. Cell 111, 5-7 (2002).
    • (2002) Cell , vol.111 , pp. 5-7
    • Yeates, T.O.1
  • 26
    • 0001067511 scopus 로고
    • Posttranslational modifications in the amino-terminal region of the large subunit of ributose-1,5-bisphosphate carboxylase/oxygenase from several plant species
    • Houtz, R.L., Poneleit, L., Jones, S.B., Royer, M. & Stults, J.T. Posttranslational modifications in the amino-terminal region of the large subunit of ributose-1,5-bisphosphate carboxylase/oxygenase from several plant species. Plant Physiol. 98, 1170-1174 (1992).
    • (1992) Plant Physiol. , vol.98 , pp. 1170-1174
    • Houtz, R.L.1    Poneleit, L.2    Jones, S.B.3    Royer, M.4    Stults, J.T.5
  • 27
    • 0000813771 scopus 로고
    • Partial purification and characterization of ribulose 1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase
    • Houtz, R.L., Royer, M. & Salvucci, M.E. Partial purification and characterization of ribulose 1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase. Plant Physiol. 97, 913-920 (1991).
    • (1991) Plant Physiol. , vol.97 , pp. 913-920
    • Houtz, R.L.1    Royer, M.2    Salvucci, M.E.3
  • 28
    • 0003518480 scopus 로고
    • John Wiley & Sons, New York
    • Segel, I.H. Enzyme Kinetics (John Wiley & Sons, New York; 1975).
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 29
    • 0028978764 scopus 로고
    • The occurrence of C-H⋯O hydrogen bonds in proteins
    • Derewenda, Z.S., Lee, L. & Derewenda, U. The occurrence of C-H⋯O hydrogen bonds in proteins. J. Mol. Biol. 252, 248-262 (1995).
    • (1995) J. Mol. Biol. , vol.252 , pp. 248-262
    • Derewenda, Z.S.1    Lee, L.2    Derewenda, U.3
  • 30
    • 0030582683 scopus 로고    scopus 로고
    • Crystallographic evidence for Cα-H⋯O=C hydrogen bonds in a collagen triple helix
    • Bella, J. & Berman, H.M. Crystallographic evidence for Cα-H⋯O=C hydrogen bonds in a collagen triple helix. J. Mol. Biol. 264, 734-742 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 734-742
    • Bella, J.1    Berman, H.M.2
  • 33
    • 0035979146 scopus 로고    scopus 로고
    • The Cα-H⋯O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes, A., Ubarretxena-Belandia, I. & Engelman, D.M. The Cα-H⋯O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Pro. Natl. Acad. Sci. USA 98, 9056-9061 (2001).
    • (2001) Pro. Natl. Acad. Sci. USA , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 35
    • 0035971221 scopus 로고    scopus 로고
    • Strength of the Cα-H⋯O hydrogen bond of amino acid residues
    • Scheiner, S., Kar, T. & Gu, Y. Strength of the Cα-H⋯O hydrogen bond of amino acid residues. J. Biol. Chem. 276, 9832-9837 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 9832-9837
    • Scheiner, S.1    Kar, T.2    Gu, Y.3
  • 36
    • 0028168468 scopus 로고
    • (His)Cε-H⋯O=C < hydrogen bond in the active sites of serine hydrolases
    • Derewenda, Z.S., Derewenda, U. & Kobos, P.M. (His)Cε-H⋯O=C < hydrogen bond in the active sites of serine hydrolases. J. Mol. Biol. 241, 83-93 (1994).
    • (1994) J. Mol. Biol. , vol.241 , pp. 83-93
    • Derewenda, Z.S.1    Derewenda, U.2    Kobos, P.M.3
  • 37
    • 0037172122 scopus 로고    scopus 로고
    • C-H⋯carboxylate oxygen hydrogen bonding in substrate activation by acyl-CoA dehydrogenases: Synergy between the H-bonds
    • Bach, R.D., Thorpe, C., & Dmitrenko, O. C-H⋯carboxylate oxygen hydrogen bonding in substrate activation by acyl-CoA dehydrogenases: synergy between the H-bonds. J. Phys. Chem. 106, 4325-4335 (2002).
    • (2002) J. Phys. Chem. , vol.106 , pp. 4325-4335
    • Bach, R.D.1    Thorpe, C.2    Dmitrenko, O.3
  • 38
    • 0002230361 scopus 로고
    • Chemical mechanisms of methyl transfer reactions: Comparison of methylases with nonenyzmatic 'model reactions'
    • eds. Salvatore, F., Borek, E., Zappia, V., William-Ashman, H.G. & Schlenk, F., Columbia University Press, New York
    • Coward, J.K. Chemical mechanisms of methyl transfer reactions: comparison of methylases with nonenyzmatic 'model reactions' in The Biochemistry of Adenosylmethionine (eds. Salvatore, F., Borek, E., Zappia, V., William-Ashman, H.G. & Schlenk, F.) 127-144 (Columbia University Press, New York; 1977).
    • (1977) The Biochemistry of Adenosylmethionine , pp. 127-144
    • Coward, J.K.1
  • 39
    • 0034685616 scopus 로고    scopus 로고
    • The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate
    • Duff, A.P., Andrews, T.J. & Curmi, P.M. The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate. J. Mol. Biol. 298, 903-916 (2000).
    • (2000) J. Mol. Biol. , vol.298 , pp. 903-916
    • Duff, A.P.1    Andrews, T.J.2    Curmi, P.M.3
  • 40
    • 0017127461 scopus 로고
    • Carnitine biosynthesis in Neurospora crassa: Enzymatic conversion of lysine to ε-N-trimethyllysine
    • Rebouche, C.J. & Broquist, H.P. Carnitine biosynthesis in Neurospora crassa: enzymatic conversion of lysine to ε-N-trimethyllysine. J. Bacteriol. 126, 1207-1214 (1976).
    • (1976) J. Bacteriol. , vol.126 , pp. 1207-1214
    • Rebouche, C.J.1    Broquist, H.P.2
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 43
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 44
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132-134 (1997).
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 45
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D 55, 938-940 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 46
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular graphics
    • Merritt, E.A. & Bacon, D.J. Raster3D version 2.0: a program for photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 47
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M.C. SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 48
    • 0001513484 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 24, 946-950 (1993).
    • (1993) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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