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Volumn 44, Issue 43, 2005, Pages 14248-14255

Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; DISSOCIATION; HYDROGEN BONDS; INTERFACES (MATERIALS); IONIZATION; PH EFFECTS; PROTEINS; TITRATION;

EID: 27444442808     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0512694     Document Type: Article
Times cited : (35)

References (40)
  • 1
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • Vallee, R. B., Williams, J. C., Varma, D., and Barnhart, L. E. (2004) Dynein: An ancient motor protein involved in multiple modes of transport, J. Neurobiol. 58, 189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 2
    • 0032583170 scopus 로고    scopus 로고
    • The 8-kDa cytoplasmic dynein light chain is required for nuclear migration and for heavy chain localization in Aspergillus nidulans
    • Beckwith, S. M., Roghi, C. H., Liu, B., and Morris, N. R. (1998) The 8-kDa cytoplasmic dynein light chain is required for nuclear migration and for heavy chain localization in Aspergillus nidulans, J. Cell Biol. 143, 1239-1247.
    • (1998) J. Cell Biol. , vol.143 , pp. 1239-1247
    • Beckwith, S.M.1    Roghi, C.H.2    Liu, B.3    Morris, N.R.4
  • 3
    • 0031777851 scopus 로고    scopus 로고
    • A dynein light chain is essential for the retrograde particle movement of intraflagellar transport (IFT)
    • Pazour, G. J., Wilkerson, C. G., and Witman, G. B. (1998) A dynein light chain is essential for the retrograde particle movement of intraflagellar transport (IFT), J. Cell Biol. 141, 979.
    • (1998) J. Cell Biol. , vol.141 , pp. 979
    • Pazour, G.J.1    Wilkerson, C.G.2    Witman, G.B.3
  • 4
    • 0029977560 scopus 로고    scopus 로고
    • Cytoplasmic dynein (ddlcl) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster
    • Dick, T., Ray, K., Salz, H. K., and Chia, W. (1996) Cytoplasmic dynein (ddlcl) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster, Mol. Cell. Biol. 16, 1966-1977.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1966-1977
    • Dick, T.1    Ray, K.2    Salz, H.K.3    Chia, W.4
  • 5
    • 27444444613 scopus 로고    scopus 로고
    • The 8 kDa dynein light chain binds to 53BP1 and mediates DNA damage-induced p53 nuclear accumulation
    • Lo, K. W., Kan, H. M., Chan, L. N., Xu, W. G., Wang, K. P., Wu, Z., Sheng, M., and Zhang, M. (2004) The 8 kDa dynein light chain binds to 53BP1 and mediates DNA damage-induced p53 nuclear accumulation, J. Biol. Chem.
    • (2004) J. Biol. Chem.
    • Lo, K.W.1    Kan, H.M.2    Chan, L.N.3    Xu, W.G.4    Wang, K.P.5    Wu, Z.6    Sheng, M.7    Zhang, M.8
  • 8
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey, S. R., and Snyder, S. H. (1996) PIN: An associated protein inhibitor of neuronal nitric oxide synthase, Science 274, 774-777.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 9
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting Swallow and the bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer, F., Bohmann, K., and Nusslein-Volhard, C. (2000) The molecular motor dynein is involved in targeting Swallow and the bicoid RNA to the anterior pole of Drosophila oocytes, Nat. Cell Biol. 2, 185-190.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 10
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath, H., Huang, D. C. S., O'Reilly, L. A., King, S. M., and Strasser, A. (1999) The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex, Mol. Cell 3, 287-296.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.S.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 11
    • 0038006754 scopus 로고    scopus 로고
    • Nuclear interaction of the dynein light chain LC8a with the TRPS1 transcription factor suppresses the transcriptional repression activity of TRPS1
    • Kaiser, F. J., Tavassoli, K., van den Bernd, G. J., Chang, G. T. G., Horsthemke, B., Moray, T., and Ludecke, H. J. (2003) Nuclear interaction of the dynein light chain LC8a with the TRPS1 transcription factor suppresses the transcriptional repression activity of TRPS1, Hum. Mol. Genet 12, 1349-1358.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 1349-1358
    • Kaiser, F.J.1    Tavassoli, K.2    Van Den Bernd, G.J.3    Chang, G.T.G.4    Horsthemke, B.5    Moray, T.6    Ludecke, H.J.7
  • 13
    • 0033776043 scopus 로고    scopus 로고
    • Interaction of the rabies virus P protein with the LC8 dynein light chain
    • Raux, H., Flamand, A., and Blondel, D. (2000) Interaction of the rabies virus P protein with the LC8 dynein light chain, J. Virol. 74, 10212-10216.
    • (2000) J. Virol. , vol.74 , pp. 10212-10216
    • Raux, H.1    Flamand, A.2    Blondel, D.3
  • 14
    • 0033775766 scopus 로고    scopus 로고
    • Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
    • Jacob, Y., Badrane, H., Ceccaldi, P. E., and Tordo, N. (2000) Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein, J. Virol. 74, 10217-10222.
    • (2000) J. Virol. , vol.74 , pp. 10217-10222
    • Jacob, Y.1    Badrane, H.2    Ceccaldi, P.E.3    Tordo, N.4
  • 15
    • 0035830488 scopus 로고    scopus 로고
    • Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain
    • Fan, J. S., Zhang, Q., Tochio, H., Li, M., and Zhang, M. J. (2001) Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain, J. Mol. Biol. 306, 97-108.
    • (2001) J. Mol. Biol. , vol.306 , pp. 97-108
    • Fan, J.S.1    Zhang, Q.2    Tochio, H.3    Li, M.4    Zhang, M.J.5
  • 16
    • 0034677929 scopus 로고    scopus 로고
    • The dynein microtubule motor
    • King, S. M. (2000) The dynein microtubule motor, Biochim. Biophys. Acta 1496, 60-75.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 60-75
    • King, S.M.1
  • 17
    • 13844275995 scopus 로고    scopus 로고
    • Solution structure of the Tctex 1 dimer reveals a mechanism for dynein-cargo interactions
    • Wu, H., Maciejewski, M. W., Takebe, S., and King, S. M. (2005) Solution structure of the Tctex 1 dimer reveals a mechanism for dynein-cargo interactions, Structure 13, 213-223.
    • (2005) Structure , vol.13 , pp. 213-223
    • Wu, H.1    Maciejewski, M.W.2    Takebe, S.3    King, S.M.4
  • 18
    • 0037006969 scopus 로고    scopus 로고
    • Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74
    • Makokha, M., Hare, M., Li, M. G., Hays, T., and Barbar, E. (2002) Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74, Biochemistry 41, 4302-4311.
    • (2002) Biochemistry , vol.41 , pp. 4302-4311
    • Makokha, M.1    Hare, M.2    Li, M.G.3    Hays, T.4    Barbar, E.5
  • 19
    • 1342299402 scopus 로고    scopus 로고
    • Interactions of LC8 with N-terminal segments of the intermediate chain of cytoplasmic dynein
    • Nyarko, A., Hare, M., Makokha, M., and Barbar, E. (2003) Interactions of LC8 with N-terminal segments of the intermediate chain of cytoplasmic dynein, Scientific World J. 3, 647-658.
    • (2003) Scientific World J. , vol.3 , pp. 647-658
    • Nyarko, A.1    Hare, M.2    Makokha, M.3    Barbar, E.4
  • 20
    • 10644253619 scopus 로고    scopus 로고
    • The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8
    • Nyarko, A., Hare, M., Hays, T. S., and Barbar, E. (2004) The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8, Biochemistry 43, 15595-15603.
    • (2004) Biochemistry , vol.43 , pp. 15595-15603
    • Nyarko, A.1    Hare, M.2    Hays, T.S.3    Barbar, E.4
  • 21
    • 10644221806 scopus 로고    scopus 로고
    • Dynein light chain LC8 promotes the assembly of the coiled coil domain of swallow protein
    • Wang, L., Hare, M., Hays, T., and Barbar, E. (2004) Dynein light chain LC8 promotes the assembly of the coiled coil domain of swallow protein, Biochemistry 43, 4611-4620.
    • (2004) Biochemistry , vol.43 , pp. 4611-4620
    • Wang, L.1    Hare, M.2    Hays, T.3    Barbar, E.4
  • 22
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif
    • Lo, K. W. H., Naisbitt, S., Fan, J. S., Sheng, M., and Zhang, M. J. (2001) The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif, J. Biol. Chem. 276, 14059-14066.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14059-14066
    • Lo, K.W.H.1    Naisbitt, S.2    Fan, J.S.3    Sheng, M.4    Zhang, M.J.5
  • 24
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar, E., Kleinman, B., Imhoff, D., Li, M. G., Hays, T. S., and Hare, M. (2001) Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein, Biochemistry 40, 1596-1605.
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.G.4    Hays, T.S.5    Hare, M.6
  • 25
    • 1342331844 scopus 로고    scopus 로고
    • The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila
    • Makokha, M., Huang, Y. J., Montelione, G., Edison, A. S., and Barbar, E. (2004) The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila, Protein Sci. 13, 727-734.
    • (2004) Protein Sci. , vol.13 , pp. 727-734
    • Makokha, M.1    Huang, Y.J.2    Montelione, G.3    Edison, A.S.4    Barbar, E.5
  • 26
    • 0029400480 scopus 로고
    • NMRPipe-A multidimensional spectral processing system based on unix pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe-A multidimensional spectral processing system based on unix pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 27
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules, Methods Mol. Biol. 278, 313-352.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 29
    • 0037452862 scopus 로고    scopus 로고
    • NMR determination of p/G values for Asp, Glu, His, and Lys mutants at each variable contiguous enzyme-inhibitor contact position of the turkey ovomucoid third domain
    • Song, J., Laskowski, M., Jr., Qasim, M. A., and Markley, J. L. (2003) NMR determination of p/G values for Asp, Glu, His, and Lys mutants at each variable contiguous enzyme-inhibitor contact position of the turkey ovomucoid third domain, Biochemistry 42, 2847-2856.
    • (2003) Biochemistry , vol.42 , pp. 2847-2856
    • Song, J.1    Laskowski Jr., M.2    Qasim, M.A.3    Markley, J.L.4
  • 30
    • 0016712920 scopus 로고
    • Nuclear magnetic resonance studies of the copper binding sites of blue copper proteins: Oxidized, reduced, and apoplastocyanin
    • Markley, J. L., Ulrich, E. L., Berg, S. P., and Krogmann, D. W. (1975) Nuclear magnetic resonance studies of the copper binding sites of blue copper proteins: Oxidized, reduced, and apoplastocyanin, Biochemistry 14, 4428-4433.
    • (1975) Biochemistry , vol.14 , pp. 4428-4433
    • Markley, J.L.1    Ulrich, E.L.2    Berg, S.P.3    Krogmann, D.W.4
  • 32
    • 0032537485 scopus 로고    scopus 로고
    • Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain
    • Forsyth, W. R., Gilson, M. K., Antosiewicz, J., Jaren, O. R., and Robertson, A. D. (1998) Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain, Biochemistry 37, 8643-8652.
    • (1998) Biochemistry , vol.37 , pp. 8643-8652
    • Forsyth, W.R.1    Gilson, M.K.2    Antosiewicz, J.3    Jaren, O.R.4    Robertson, A.D.5
  • 33
    • 0027456412 scopus 로고
    • Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • Pelton, J. G., Torchia, D. A., Meadow, N. D., and Roseman, S. (1993) Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques, Protein Sci. 2, 543-558.
    • (1993) Protein Sci. , vol.2 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 35
    • 0142039800 scopus 로고    scopus 로고
    • Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly
    • Wang, W., Lo, K. W., Kan, H. M., Fan, J. S., and Zhang, M. (2003) Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly, J. Biol. Chem. 278, 41491-41499.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41491-41499
    • Wang, W.1    Lo, K.W.2    Kan, H.M.3    Fan, J.S.4    Zhang, M.5
  • 37
    • 0036783381 scopus 로고    scopus 로고
    • a of histidine side-chains correlates with burial within proteins
    • a of histidine side-chains correlates with burial within proteins, Proteins 49, 1-6.
    • (2002) Proteins , vol.49 , pp. 1-6
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 38
    • 0028170657 scopus 로고
    • pH titration of the histidine residues of cyclophilin and FK506 binding protein in the absence and presence of immunosuppressant ligands
    • Yu, L., and Fesik, S. W. (1994) pH titration of the histidine residues of cyclophilin and FK506 binding protein in the absence and presence of immunosuppressant ligands, Biochim. Biophys. Acta 1209, 24-32.
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 24-32
    • Yu, L.1    Fesik, S.W.2
  • 39
    • 0029843569 scopus 로고    scopus 로고
    • Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange
    • Plesniak, L. A., Connelly, G. P., Wakarchuk, W. W., and McIntosh, L. P. (1996) Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange, Protein Sci. 5, 2319-2328.
    • (1996) Protein Sci. , vol.5 , pp. 2319-2328
    • Plesniak, L.A.1    Connelly, G.P.2    Wakarchuk, W.W.3    McIntosh, L.P.4


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