메뉴 건너뛰기




Volumn 1838, Issue 1 PARTB, 2014, Pages 413-418

Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy

Author keywords

Amphipathic helix; Chloroplast TatB; Membrane active peptide; Twin arginine transport

Indexed keywords

GALACTOSYLDIACYLGLYCEROL; MEMBRANE PROTEIN; PHOSPHOLIPID; PROTEIN HCF106; UNCLASSIFIED DRUG;

EID: 84887870763     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.10.007     Document Type: Article
Times cited : (10)

References (38)
  • 1
    • 84871749722 scopus 로고    scopus 로고
    • The chloroplast protein import system: From algae to trees
    • L.X. Shi, and S.M. Theg The chloroplast protein import system: from algae to trees BBA Mol. Cell Res. 1833 2013 314 331
    • (2013) BBA Mol. Cell Res. , vol.1833 , pp. 314-331
    • Shi, L.X.1    Theg, S.M.2
  • 2
    • 84871734172 scopus 로고    scopus 로고
    • Intra-plastid protein trafficking: How plant cells adapted prokaryotic mechanisms to the eukaryotic condition
    • J.M. Celedon, and K. Cline Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition BBA Mol. Cell Res. 1833 2013 341 351
    • (2013) BBA Mol. Cell Res. , vol.1833 , pp. 341-351
    • Celedon, J.M.1    Cline, K.2
  • 3
    • 56349086943 scopus 로고    scopus 로고
    • Plastid protein import and sorting: Different paths to the same compartments
    • K. Cline, and C. Dabney-Smith Plastid protein import and sorting: different paths to the same compartments Curr. Opin. Plant Biol. 11 2008 585 592
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 585-592
    • Cline, K.1    Dabney-Smith, C.2
  • 4
    • 0348140629 scopus 로고    scopus 로고
    • Functional assembly of thylakoid ΔpH-dependent/Tat protein transport pathway components in vitro
    • DOI 10.1046/j.1432-1033.2003.03894.x
    • V. Fincher, C. Dabney-Smith, and K. Cline Functional assembly of thylakoid deltapH-dependent/Tat protein transport pathway components in vitro Eur. J. Biochem. 270 2003 4930 4941 (Pubitemid 38021575)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.24 , pp. 4930-4941
    • Fincher, V.1    Dabney-Smith, C.2    Cline, K.3
  • 5
    • 78449239236 scopus 로고    scopus 로고
    • Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis
    • Y. Hu, E. Zhao, H. Li, B. Xia, and C. Jin Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis J. Am. Chem. Soc. 132 2010 15942 15944
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15942-15944
    • Hu, Y.1    Zhao, E.2    Li, H.3    Xia, B.4    Jin, C.5
  • 6
    • 78449242888 scopus 로고    scopus 로고
    • Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy
    • T.H. Walther, S.L. Grage, N. Roth, and A.S. Ulrich Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy J. Am. Chem. Soc. 132 2010 15945 15956
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15945-15956
    • Walther, T.H.1    Grage, S.L.2    Roth, N.3    Ulrich, A.S.4
  • 7
    • 0035854799 scopus 로고    scopus 로고
    • Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport
    • PII S0014579301026266
    • H. Mori, E.J. Summer, and K. Cline Chloroplast TatC plays a direct role in thylakoid (Delta)pH-dependent protein transport FEBS Lett. 501 2001 65 68 (Pubitemid 33712488)
    • (2001) FEBS Letters , vol.501 , Issue.1-3 , pp. 65-68
    • Mori, H.1    Summer, E.J.2    Cline, K.3
  • 9
    • 66249084873 scopus 로고    scopus 로고
    • Localization and integration of thylakoid protein translocase subunit cpTatC
    • J.R. Martin, J.H. Harwood, M. McCaffery, D.E. Fernandez, and K. Cline Localization and integration of thylakoid protein translocase subunit cpTatC Plant J. 58 2009 831 842
    • (2009) Plant J. , vol.58 , pp. 831-842
    • Martin, J.R.1    Harwood, J.H.2    McCaffery, M.3    Fernandez, D.E.4    Cline, K.5
  • 10
    • 0028025665 scopus 로고
    • Solid-state NMR structural studies of peptides and proteins in membranes
    • T.A. Cross, and S.J. Opella Solid-state NMR structural studies of peptides and proteins in membranes Curr. Opin. Struct. Biol. 4 1994 574 581 (Pubitemid 24268991)
    • (1994) Current Opinion in Structural Biology , vol.4 , Issue.4 , pp. 574-581
    • Cross, T.A.1    Opella, S.J.2
  • 11
    • 0038451228 scopus 로고    scopus 로고
    • Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods
    • DOI 10.1021/ja0300721
    • Y. Nakazawa, and T. Asakura Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods J. Am. Chem. Soc. 125 2003 7230 7237 (Pubitemid 36798970)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.24 , pp. 7230-7237
    • Nakazawa, Y.1    Asakura, T.2
  • 12
    • 0031740077 scopus 로고    scopus 로고
    • Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes
    • DOI 10.1016/S0304-4157(98)00012-4, PII S0304415798000124
    • A. Watts Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes Biochim. Biophys. Acta 1376 1998 297 318 (Pubitemid 28517882)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 297-318
    • Watts, A.1
  • 13
    • 33750707584 scopus 로고    scopus 로고
    • 13C solid-state NMR spectroscopic study
    • DOI 10.1021/bi0614028
    • S. Abu-Baker, and G.A. Lorigan Phospholamban and its phosphorylated form interact differently with lipid bilayers: a 31P, 2H, and 13C solid-state NMR spectroscopic study Biochemistry 45 2006 13312 13322 (Pubitemid 44707691)
    • (2006) Biochemistry , vol.45 , Issue.44 , pp. 13312-13322
    • Abu-Baker, S.1    Lorigan, G.A.2
  • 15
    • 1542345586 scopus 로고    scopus 로고
    • 31P and 2H solid-state NMR spectroscopic studies of the transmembrane domain of the membrane-bound protein phospholamban
    • P.C. Dave, E.K. Tiburu, K. Damodaran, and G.A. Lorigan 31P and 2H solid-state NMR spectroscopic studies of the transmembrane domain of the membrane-bound protein phospholamban Biophys. J. 86 2004 1564 1573
    • (2004) Biophys. J. , vol.86 , pp. 1564-1573
    • Dave, P.C.1    Tiburu, E.K.2    Damodaran, K.3    Lorigan, G.A.4
  • 16
    • 0842286082 scopus 로고    scopus 로고
    • Effects of antidepressants on the conformation of phospholipid headgroups studied by solid-state NMR
    • DOI 10.1002/mrc.1327
    • J.S. Santos, D.K. Lee, and A. Ramamoorthy Effects of antidepressants on the conformation of phospholipid headgroups studied by solid-state NMR Magn. Reson. Chem. 42 2004 105 114 (Pubitemid 38178078)
    • (2004) Magnetic Resonance in Chemistry , vol.42 , Issue.2 , pp. 105-114
    • Santos, J.S.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 17
    • 0033545957 scopus 로고    scopus 로고
    • Site-specific deuterium order parameters and membrane-bound behavior of a peptide fragment from the intracellular domain of HIV-1 gp41
    • B.W. Koenig, J.A. Ferretti, and K. Gawrisch Site-specific deuterium order parameters and membrane-bound behavior of a peptide fragment from the intracellular domain of HIV-1 gp41 Biochemistry 38 1999 6327 6334
    • (1999) Biochemistry , vol.38 , pp. 6327-6334
    • Koenig, B.W.1    Ferretti, J.A.2    Gawrisch, K.3
  • 18
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • S. Yamaguchi, D. Huster, A. Waring, R.I. Lehrer, W. Kearney, B.F. Tack, and M. Hong Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy Biophys. J. 81 2001 2203 2214 (Pubitemid 32917169)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 19
    • 23044450818 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer membranes
    • DOI 10.1021/bi050730p
    • J.X. Lu, K. Damodaran, J. Blazyk, and G.A. Lorigan Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer membranes Biochemistry 44 2005 10208 10217 (Pubitemid 41076816)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10208-10217
    • Lu, J.-X.1    Damodaraiv, K.2    Blazyk, J.3    Lorigan, G.A.4
  • 20
    • 0035443197 scopus 로고    scopus 로고
    • Biophysical approaches to membrane protein structure determination
    • DOI 10.1016/S0959-440X(00)00246-3
    • A. Arora, and L.K. Tamm Biophysical approaches to membrane protein structure determination Curr. Opin. Struct. Biol. 11 2001 540 547 (Pubitemid 32972014)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.5 , pp. 540-547
    • Arora, A.1    Tamm, L.K.2
  • 21
    • 0019877811 scopus 로고
    • Protein-lipid interactions: Do the spectroscopists now agree?
    • A. Watts Protein-lipid interactions: do the spectroscopists now agree? Nature 294 1981 512 513
    • (1981) Nature , vol.294 , pp. 512-513
    • Watts, A.1
  • 22
    • 0028235050 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • DOI 10.1016/0014-5793(94)00467-6
    • M.A. Lemmon, and D.M. Engelman Specificity and promiscuity in membrane helix interactions FEBS Lett. 346 1994 17 20 (Pubitemid 24183820)
    • (1994) FEBS Letters , vol.346 , Issue.1 , pp. 17-20
    • Lemmon, M.A.1
  • 23
    • 0025993884 scopus 로고
    • Physical properties of the fluid lipid-bilayer component of cell membranes: A perspective
    • M. Bloom, E. Evans, and O.G. Mouritsen Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective Q. Rev. Biophys. 24 1991 293 397 (Pubitemid 121000390)
    • (1991) Quarterly Reviews of Biophysics , vol.24 , Issue.3 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 25
    • 0017252285 scopus 로고
    • Molecular motion and order in single-bilayer vesicles and multilamellar dispersions of egg lecithin and lecithin-cholesterol mixtures. A deuterium nuclear magnetic resonance study of specifically labeled lipids
    • G.W. Stockton, C.F. Polnaszek, A.P. Tulloch, F. Hasan, and I.C. Smith Molecular motion and order in single-bilayer vesicles and multilamellar dispersions of egg lecithin and lecithin-cholesterol mixtures. A deuterium nuclear magnetic resonance study of specifically labeled lipids Biochemistry 15 1976 954 966
    • (1976) Biochemistry , vol.15 , pp. 954-966
    • Stockton, G.W.1    Polnaszek, C.F.2    Tulloch, A.P.3    Hasan, F.4    Smith, I.C.5
  • 26
    • 0037686414 scopus 로고    scopus 로고
    • An improved synthetic and purification procedure for the hydrophobic segment of the transmembrane peptide phospholamban
    • DOI 10.1016/S0003-2697(03)00141-6
    • E.K. Tiburu, P.C. Dave, J.F. Vanlerberghe, T.B. Cardon, R.E. Minto, and G.A. Lorigan An improved synthetic and purification procedure for the hydrophobic segment of the transmembrane peptide phospholamban Anal. Biochem. 318 2003 146 151 (Pubitemid 36627494)
    • (2003) Analytical Biochemistry , vol.318 , Issue.1 , pp. 146-151
    • Tiburu, E.K.1    Dave, P.C.2    Vanlerberghe, J.F.3    Cardon, T.B.4    Minto, R.E.5    Lorigan, G.A.6
  • 28
    • 1842783195 scopus 로고    scopus 로고
    • The effects of cholesterol on magnetically aligned phospholipid bilayers: A solid-state NMR and EPR spectroscopy study
    • J.-X. Lu, M.A. Caporini, and G.A. Lorigan The effects of cholesterol on magnetically aligned phospholipid bilayers: a solid-state NMR and EPR spectroscopy study J. Magn. Reson. 168 2004 18 30
    • (2004) J. Magn. Reson. , vol.168 , pp. 18-30
    • Lu, J.-X.1    Caporini, M.A.2    Lorigan, G.A.3
  • 29
    • 0017902280 scopus 로고
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • J. Seelig 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes Biochim. Biophys. Acta 515 1978 105 140 (Pubitemid 8398025)
    • (1978) Biochimica et Biophysica Acta , vol.515 , Issue.2 , pp. 105-140
    • Seelig, J.1
  • 30
    • 0025224152 scopus 로고
    • Biochemistry and function of the plastid envelope
    • R. Douce, and J. Joyard Biochemistry and function of the plastid envelope Annu. Rev. Cell Biol. 6 1990 173 216
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 173-216
    • Douce, R.1    Joyard, J.2
  • 31
    • 1542345586 scopus 로고    scopus 로고
    • 2H Solid-State NMR Spectroscopy
    • P.C. Dave, E.K. Tiburu, K. Damodaran, and G.A. Lorigan Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing P-31 and H-2 solid-state NMR spectroscopy Biophys. J. 86 2004 1564 1573 (Pubitemid 38295591)
    • (2004) Biophysical Journal , vol.86 , Issue.3 , pp. 1564-1573
    • Dave, P.C.1    Tiburu, E.K.2    Damodaran, K.3    Lorigan, G.A.4
  • 32
    • 0017580849 scopus 로고
    • 31P nuclear magnetic resonance chemical shielding tensors
    • DOI 10.1021/bi00622a028
    • S.J. Kohler, and M.P. Klein Orientation and dynamics of phospholipid head groups in bilayers and membranes determined from P-31 nuclear magnetic-resonance chemical shielding tensors Biochemistry 16 1977 519 526 (Pubitemid 8036387)
    • (1977) Biochemistry , vol.16 , Issue.3 , pp. 519-526
    • Kohler, S.J.1    Klein, M.P.2
  • 33
    • 27844483368 scopus 로고    scopus 로고
    • 2H solid-state NMR spectroscopy
    • DOI 10.1016/j.bbamem.2005.09.014, PII S0005273605002877
    • S. Abu-Baker, X. Qi, J. Newstadt, and G.A. Lorigan Structural changes in a binary mixed phospholipid bilayer of DOPG and DOPS upon saposin C interaction at acidic pH utilizing 31P and 2H solid-state NMR spectroscopy Biochim. Biophys. Acta 1717 2005 58 66 (Pubitemid 41642666)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1717 , Issue.1 , pp. 58-66
    • Abu-Baker, S.1    Qi, X.2    Newstadt, J.3    Lorigan, G.A.4
  • 34
    • 30844466828 scopus 로고    scopus 로고
    • 13C heteronuclear dipolar solid-state NMR spectroscopy
    • DOI 10.1016/j.jmr.2005.09.006, PII S1090780705003083
    • J.X. Lu, K. Damodaran, and G.A. Lorigan Probing membrane topology by high-resolution 1H-13C heteronuclear dipolar solid-state NMR spectroscopy J. Magn. Reson. 178 2006 283 287 (Pubitemid 43107934)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.2 , pp. 283-287
    • Lu, J.-X.1    Damodaran, K.2    Lorigan, G.A.3
  • 36
    • 0017822501 scopus 로고
    • Head-group conformation in phospholipids: A phosphorus-31 nuclear magnetic resonance study of oriented monodomain dipalmitoylphosphatidylcholine bilayers
    • R.G. Griffin, L. Powers, and P.S. Pershan Head-group conformation in phospholipids - P-31 nuclear magnetic-resonance study of oriented monodomain dipalmitoylphosphatidylcholine bilayers Biochemistry 17 1978 2718 2722 (Pubitemid 8385269)
    • (1978) Biochemistry , vol.17 , Issue.14 , pp. 2718-2722
    • Griffin, R.G.1    Powers, L.2    Pershan, P.S.3
  • 37
    • 0016283654 scopus 로고
    • The dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance
    • A. Seelig, and J. Seelig The dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance Biochemistry 13 1974 4839 4845
    • (1974) Biochemistry , vol.13 , pp. 4839-4845
    • Seelig, A.1    Seelig, J.2
  • 38
    • 0015981720 scopus 로고
    • Deuterium magnetic resonance studies of phospholipid bilayers
    • J. Seelig, and A. Seelig Deuterium magnetic resonance studies of phospholipid bilayers Biochem. Biophys. Res. Commun. 57 1974 406 411
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 406-411
    • Seelig, J.1    Seelig, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.