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Volumn 48, Issue 47, 2009, Pages 11185-11195

Interaction of the Tim44 C-terminal domain with negatively charged phospholipids

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PHOSPHOLIPIDS; C-TERMINAL DOMAINS; CARBOXY-TERMINAL DOMAINS; CARDIOLIPINS; CYTOSOLS; DIRECT INTERACTIONS; HIGH-RESOLUTION STRUCTURES; HYDROPHOBIC CAVITIES; HYDROPHOBIC TAILS; IN-VITRO; INNER MEMBRANES; MITOCHONDRIAL MATRIX; MITOCHONDRIAL PROTEIN; MODEL MEMBRANES; MOLECULAR DYNAMICS SIMULATIONS; N-TERMINAL TRUNCATION; N-TERMINALS; OUTER MEMBRANE; PHOSPHOLIPID VESICLES; PROTEIN IMPORT; RECOGNITION SITE;

EID: 72749116151     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900998v     Document Type: Article
Times cited : (32)

References (45)
  • 1
    • 27744543167 scopus 로고    scopus 로고
    • How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
    • Rapaport, D. (2005) How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane? J. Cell Biol. 171, 419-423.
    • (2005) J. Cell Biol , vol.171 , pp. 419-423
    • Rapaport, D.1
  • 2
    • 27844535385 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Mokranjac, D., and Neupert, W. (2005) Protein import into mitochondria. Biochem. Soc. Trans. 33, 1019-1023.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1019-1023
    • Mokranjac, D.1    Neupert, W.2
  • 3
    • 0037009129 scopus 로고    scopus 로고
    • The mitochondrial import machinery: Preprotein-conducting channels with binding sites for presequences
    • Pfanner, N., and Chacinska, A. (2002) The mitochondrial import machinery: Preprotein-conducting channels with binding sites for presequences. Biochim. Biophys. Acta 1592, 15-24.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 15-24
    • Pfanner, N.1    Chacinska, A.2
  • 7
    • 44349105790 scopus 로고    scopus 로고
    • Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria
    • DOI 10.1038/emboj.2008.79, PII EMBOJ200879
    • Popov-Celeketic, D., Mapa, K., Neupert, W., and Mokranjac, D. (2008) Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria. EMBO J. 27, 1469-1480. (Pubitemid 351733334)
    • (2008) EMBO Journal , vol.27 , Issue.10 , pp. 1469-1480
    • Popov-Celeketic, D.1    Mapa, K.2    Neupert, W.3    Mokranjac, D.4
  • 9
    • 21244458136 scopus 로고    scopus 로고
    • Role of Tim21 in mitochondrial translocation contact sites
    • Mokranjac, D., Popov-Celeketic, D., Hell, K., and Neupert, W. (2005) Role of Tim21 in mitochondrial translocation contact sites. J. Biol. Chem. 280, 23437-23440.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23437-23440
    • Mokranjac, D.1    Popov-Celeketic, D.2    Hell, K.3    Neupert, W.4
  • 12
    • 61449229779 scopus 로고    scopus 로고
    • The genetic interactome of prohibitins: Coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria
    • Osman, C., Haag, M., Potting, C., Rodenfels, J., Dip, P. V., Wieland, F. T., Brugger, B., Westermann, B., and Langer, T. (2009) The genetic interactome of prohibitins: Coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J. Cell Biol. 184, 583-596.
    • (2009) J. Cell Biol , vol.184 , pp. 583-596
    • Osman, C.1    Haag, M.2    Potting, C.3    Rodenfels, J.4    Dip, P.V.5    Wieland, F.T.6    Brugger, B.7    Westermann, B.8    Langer, T.9
  • 14
    • 0037174138 scopus 로고    scopus 로고
    • Cardiolipin: A proton trap for oxidative phosphorylation
    • Haines, T. H., and Dencher, N. A. (2002) Cardiolipin: A proton trap for oxidative phosphorylation. FEBS Lett. 528, 35-39.
    • (2002) FEBS Lett , vol.528 , pp. 35-39
    • Haines, T.H.1    Dencher, N.A.2
  • 15
    • 33846231055 scopus 로고    scopus 로고
    • Localization of a Drosophila melanogaster homolog of the putative juvenile hormone esterase binding protein of Manduca sexta
    • Liu, Z., Ho, L., and Bonning, B. (2007) Localization of a Drosophila melanogaster homolog of the putative juvenile hormone esterase binding protein of Manduca sexta. Insect Biochem. Mol. Biol. 37, 155-163.
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 155-163
    • Liu, Z.1    Ho, L.2    Bonning, B.3
  • 16
    • 34250789163 scopus 로고    scopus 로고
    • Role of cardiolipin in cytochrome c release from mitochondria
    • DOI 10.1038/sj.cdd.4402135, PII 4402135
    • Ott, M., Zhivotovsky, B., and Orrenius, S. (2007) Role of cardiolipin in cytochrome c release from mitochondria. Cell Death Differ. 14, 1243-1247. (Pubitemid 46965253)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.7 , pp. 1243-1247
    • Ott, M.1    Zhivotovsky, B.2    Orrenius, S.3
  • 17
    • 70349557331 scopus 로고    scopus 로고
    • Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function
    • Claypool, S. M. (2009) Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function. Biochim. Biophys. Acta 1788, 2059-2068.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2059-2068
    • Claypool, S.M.1
  • 20
    • 47049119447 scopus 로고    scopus 로고
    • The essential function of Tim12 in vivo is ensured by the assembly interactions of its C-terminal domain
    • Lionaki, E., de Marcos Lousa, C., Baud, C., Vougioukalaki, M., Panayotou, G., and Tokatlidis, K. (2008) The essential function of Tim12 in vivo is ensured by the assembly interactions of its C-terminal domain. J. Biol. Chem. 283, 15747-15753.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15747-15753
    • Lionaki, E.1    De Marcos Lousa, C.2    Baud, C.3    Vougioukalaki, M.4    Panayotou, G.5    Tokatlidis, K.6
  • 22
    • 33646868373 scopus 로고    scopus 로고
    • Crystal structure of yeast mitochondrial peripheral membrane protein Tim44p C-terminal domain
    • Josyula, R., Jin, Z., Fu, Z., and Sha, B. (2006) Crystal structure of yeast mitochondrial peripheral membrane protein Tim44p C-terminal domain. J. Mol. Biol. 359, 798-804.
    • (2006) J. Mol. Biol. , vol.359 , pp. 798-804
    • Josyula, R.1    Jin, Z.2    Fu, Z.3    Sha, B.4
  • 23
    • 36349010951 scopus 로고    scopus 로고
    • The interplay between components of the mitochondrial protein translocation motor studied using purified components
    • Slutsky-Leiderman, O., Marom, M., Iosefson, O., Levy, R., Maoz, S., and Azem, A. (2007) The interplay between components of the mitochondrial protein translocation motor studied using purified components. J. Biol. Chem. 282, 33935-33942.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33935-33942
    • Slutsky-Leiderman, O.1    Marom, M.2    Iosefson, O.3    Levy, R.4    Maoz, S.5    Azem, A.6
  • 24
    • 0030841365 scopus 로고    scopus 로고
    • The mitochondrial hsp70 chaperone system. Effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70
    • Azem, A., Oppliger, W., Lustig, A., Jeno, P., Feifel, B., Schatz, G., and Horst, M. (1997) The mitochondrial hsp70 chaperone system. Effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70. J. Biol. Chem. 272, 20901-20906.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20901-20906
    • Azem, A.1    Oppliger, W.2    Lustig, A.3    Jeno, P.4    Feifel, B.5    Schatz, G.6    Horst, M.7
  • 25
    • 0031614308 scopus 로고    scopus 로고
    • Ultracentrifugation technique for measuring the binding of peptides and proteins to sucroseloaded phospholipid vesicles
    • Buser, C. A., and McLaughlin, S. (1998) Ultracentrifugation technique for measuring the binding of peptides and proteins to sucroseloaded phospholipid vesicles. Methods Mol. Biol. 84, 267-281.
    • (1998) Methods Mol. Biol , vol.84 , pp. 267-281
    • Buser, C.A.1    McLaughlin, S.2
  • 26
    • 0029147499 scopus 로고
    • The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane
    • Vergeres, G., Manenti, S., Weber, T., and Sturzinger, C. (1995) The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane. J. Biol. Chem. 270, 19879-19887.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19879-19887
    • Vergeres, G.1    Manenti, S.2    Weber, T.3    Sturzinger, C.4
  • 27
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H. J. C., van der Spoel, D., and van Drunen, R. (1995) GROMACS: A message-passing parallel molecular dynamics implementation. Comput. Phys. Commun. 91, 43-56.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 28
    • 0035789518 scopus 로고    scopus 로고
    • Gromacs 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., Hess, B., and van der Spoel, D. (2001) Gromacs 3.0: A package for molecular simulation and trajectory analysis. J. Mol. Model. 7, 306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 30
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C., Villa, A., Mark, A. E., and Van Gunsteren, W. F. (2004) A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem. 25, 1656-1676.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 32
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18, 2714-2723. (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 33
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W., and van Aalten, D. M. (2004) PRODRG: A tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D60, 1355-1363.
    • (2004) Acta Crystallogr , vol.D60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 34
    • 15544371572 scopus 로고
    • Interaction Models for Water in Relation to Protein Hydration
    • Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., and Hermans, J. (1969) Interaction Models for Water in Relation to Protein Hydration. Nature 224, 175-177.
    • (1969) Nature , vol.224 , pp. 175-177
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 35
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., Bekker, H., Berendsen, H. J. C., and Fraaije, J. G. E. M. (1997) LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463-1472.
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 36
    • 84986440341 scopus 로고
    • SETTLE: An Analytical Version of the SHAKE and RATTLE Algorithms for Rigid water models
    • Miyamoto, S., and Kollman, P. A. (1992) SETTLE: An Analytical Version of the SHAKE and RATTLE Algorithms for Rigid water models. J. Comput. Chem. 13, 952-962.
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 40
    • 15544381165 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the adipocyte lipid binding protein reveal a novel entry site for the ligand
    • DOI 10.1021/bi048236t
    • Friedman, R., Nachliel, E., and Gutman, M. (2005) Molecular Dynamics Simulations of the Adipocyte Lipid Binding Protein Reveal a Novel Entry Site for the Ligand. Biochemistry 44, 4275-4283. (Pubitemid 40403968)
    • (2005) Biochemistry , vol.44 , Issue.11 , pp. 4275-4283
    • Friedman, R.1    Nachliel, E.2    Gutman, M.3
  • 41
    • 33847760345 scopus 로고    scopus 로고
    • Molecular dynamics simulations of palmitate entry into the hydrophobic pocket of the fatty acid binding protein
    • DOI 10.1016/j.febslet.2007.02.033, PII S0014579307001986
    • Tsfadia, Y., Friedman, R., Kadmon, J., Selzer, A., Nachliel, E., and Gutman, M. (2007) Molecular dynamics simulations of palmitate entry into the hydrophobic pocket of the fatty acid binding protein. FEBS Lett. 581, 1243-1247. (Pubitemid 46385944)
    • (2007) FEBS Letters , vol.581 , Issue.6 , pp. 1243-1247
    • Tsfadia, Y.1    Friedman, R.2    Kadmon, J.3    Selzer, A.4    Nachliel, E.5    Gutman, M.6
  • 42
    • 67349282399 scopus 로고    scopus 로고
    • Molecular dynamics study of the interaction between fatty acid binding proteins with palmitate mini-micelles
    • Levin, L. B., Nachliel, E., Gutman, M., and Tsfadia, Y. (2009) Molecular dynamics study of the interaction between fatty acid binding proteins with palmitate mini-micelles. Mol. Cell. Biochem. 326, 29-33.
    • (2009) Mol. Cell. Biochem. , vol.326 , pp. 29-33
    • Levin, L.B.1    Nachliel, E.2    Gutman, M.3    Tsfadia, Y.4
  • 44
    • 67650266997 scopus 로고    scopus 로고
    • Structural and dynamic effects of cholesterol at preferred sites of interaction with rhodopsin identified from microsecond length molecular dynamics simulations
    • Khelashvili, G., Grossfield, A., Feller, S. E., Pitman, M. C., and Weinstein, H. (2009) Structural and dynamic effects of cholesterol at preferred sites of interaction with rhodopsin identified from microsecond length molecular dynamics simulations. Proteins 76, 403-417.
    • (2009) Proteins , vol.76 , pp. 403-417
    • Khelashvili, G.1    Grossfield, A.2    Feller, S.E.3    Pitman, M.C.4    Weinstein, H.5
  • 45
    • 56349144637 scopus 로고    scopus 로고
    • Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling
    • Mokranjac, D., and Neupert, W. (2009) Thirty years of protein translocation into mitochondria: Unexpectedly complex and still puzzling. Biochim. Biophys. Acta 1793, 33-41.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 33-41
    • Mokranjac, D.1    Neupert, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.