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Volumn 137, Issue 1-2, 2002, Pages 220-235

Helix capping interactions stabilize the N-terminus of the kinesin neck coiled-coil

Author keywords

Capping box; Coiled coil; Hydrophobic staple; Kinesin; N cap

Indexed keywords

ALANINE; GLYCINE; KINESIN; LEUCINE; TRYPTOPHAN;

EID: 0036445514     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2002.4475     Document Type: Conference Paper
Times cited : (22)

References (52)
  • 1
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studies with optical tweezers
    • Block, S. M., Goldstein, L. S., and Schnapp, B. J. (1990) Bead movement by single kinesin molecules studies with optical tweezers. Nature 348, 348-352.
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.2    Schnapp, B.J.3
  • 2
    • 0030874883 scopus 로고    scopus 로고
    • The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
    • Case, R. B., Pierce, D. W., Hom-Booher, N., Hart, C. L., and Vale, R. D. (1997) The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain. Cell 90, 959-966.
    • (1997) Cell , vol.90 , pp. 959-966
    • Case, R.B.1    Pierce, D.W.2    Hom-Booher, N.3    Hart, C.L.4    Vale, R.D.5
  • 3
    • 0034628619 scopus 로고    scopus 로고
    • Role of the kinesin neck linker and catalytic core in microtubule-based motility
    • Case, R. B., Rice, S., Hart, C. L., Ly, B., and Vale, R. D. (2000) Role of the kinesin neck linker and catalytic core in microtubule-based motility. Curr. Biol. 10, 157-160.
    • (2000) Curr. Biol. , vol.10 , pp. 157-160
    • Case, R.B.1    Rice, S.2    Hart, C.L.3    Ly, B.4    Vale, R.D.5
  • 4
    • 0028917410 scopus 로고
    • Sedimentation studies on the kinesin motor domain constructs K401, K366, and K341
    • Correia, J. J., Gilbert, S. P., Moyer, M. L., and Johnson, K. A. (1995) Sedimentation studies on the kinesin motor domain constructs K401, K366, and K341. Biochemistry 34, 4898-4907.
    • (1995) Biochemistry , vol.34 , pp. 4898-4907
    • Correia, J.J.1    Gilbert, S.P.2    Moyer, M.L.3    Johnson, K.A.4
  • 5
    • 0028898360 scopus 로고
    • On the hand-over-hand footsteps of kinesin heads
    • Cross, R. A. (1995) On the hand-over-hand footsteps of kinesin heads. J. Muscle Res. Cell Motil. 16, 91-94.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 91-94
    • Cross, R.A.1
  • 6
    • 0026013127 scopus 로고
    • Circular dichroism study on the conformational stability of the dimerization domain of transcription factor LFB1
    • De Francesco, R., Pastore, A., Vecchio, G., and Cortese, R. (1991) Circular dichroism study on the conformational stability of the dimerization domain of transcription factor LFB1. Biochemistry 30, 143-147.
    • (1991) Biochemistry , vol.30 , pp. 143-147
    • De Francesco, R.1    Pastore, A.2    Vecchio, G.3    Cortese, R.4
  • 7
    • 0032555532 scopus 로고    scopus 로고
    • Determinants of kinesin motor polarity
    • Endow, S. A., and Waligora, K. W. (1998) Determinants of kinesin motor polarity. Science 281, 1200-1202.
    • (1998) Science , vol.281 , pp. 1200-1202
    • Endow, S.A.1    Waligora, K.W.2
  • 8
    • 0026253633 scopus 로고
    • The helix-coil transition in heterogeneous peptides with specific side-chain interactions: Theory and comparison with CD spectral data
    • Gans, P. J., Lyu, P. C., Manning, M. C., Woody, R. W., and Kallenbach, N. R. (1991) The helix-coil transition in heterogeneous peptides with specific side-chain interactions: Theory and comparison with CD spectral data. Biopolymers 31, 1605-1614.
    • (1991) Biopolymers , vol.31 , pp. 1605-1614
    • Gans, P.J.1    Lyu, P.C.2    Manning, M.C.3    Woody, R.W.4    Kallenbach, N.R.5
  • 9
    • 0028985886 scopus 로고
    • Pathway of processive ATP hydrolysis by kinesin
    • Gilbert, S. P., Webb, M. R., Brune, M., and Johnson, K. A. (1995) Pathway of processive ATP hydrolysis by kinesin. Nature 373, 671-676.
    • (1995) Nature , vol.373 , pp. 671-676
    • Gilbert, S.P.1    Webb, M.R.2    Brune, M.3    Johnson, K.A.4
  • 10
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert, S. P., Moyer, M. L., and Johnson, K. A. (1998) Alternating site mechanism of the kinesin ATPase. Biochemistry 37, 792-799
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1    Moyer, M.L.2    Johnson, K.A.3
  • 11
    • 0033280668 scopus 로고    scopus 로고
    • The road less traveled: Emerging principles of kinesin motor utilization
    • Goldstein, L. S., and Philp, A. V. (1999) The road less traveled: Emerging principles of kinesin motor utilization. Annu. Rev. Cell. Dev. Biol. 15, 141-183.
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 141-183
    • Goldstein, L.S.1    Philp, A.V.2
  • 12
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney, D. D. (1994) Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl. Acad. Sci. USA 91, 6865-6869.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 13
    • 0029156511 scopus 로고
    • Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
    • Hackney, D. D. (1995) Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature 377, 448-450.
    • (1995) Nature , vol.377 , pp. 448-450
    • Hackney, D.D.1
  • 14
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock, W. O., and Howard, J. (1998) Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140, 1395-1405.
    • (1998) J. Cell Biol. , vol.140 , pp. 1395-1405
    • Hancock, W.O.1    Howard, J.2
  • 15
    • 0030924142 scopus 로고    scopus 로고
    • Reversal in the direction of movement of a molecular motor
    • Henningsen, U., and Schliwa, M. (1997) Reversal in the direction of movement of a molecular motor. Nature 389, 93-96.
    • (1997) Nature , vol.389 , pp. 93-96
    • Henningsen, U.1    Schliwa, M.2
  • 16
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with x-ray structure and implications for motility
    • Hoenger, A., Sack, S., Thormahlen, M., Marx, A., Muller, J., Gross, H., and Mandelkow, E. (1998) Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with x-ray structure and implications for motility. J. Cell. Biol. 141, 419-430.
    • (1998) J. Cell. Biol. , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormahlen, M.3    Marx, A.4    Muller, J.5    Gross, H.6    Mandelkow, E.7
  • 17
    • 0029960345 scopus 로고    scopus 로고
    • The movement of kinesin along microtubules
    • Howard, J. (1996) The movement of kinesin along microtubules. Annu. Rev. Physiol. 58, 703-729.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 703-729
    • Howard, J.1
  • 18
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard, J., Hudspeth, A. J., and Vale, R. D. (1989) Movement of microtubules by single kinesin molecules. Nature 342, 154-158.
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 19
    • 0028579468 scopus 로고
    • Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli
    • Huang, T. G., Suhan, J., and Hackney, D. D. (1994) Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli. J. Biol. Chem. 269, 32708.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32708
    • Huang, T.G.1    Suhan, J.2    Hackney, D.D.3
  • 21
    • 0031004867 scopus 로고    scopus 로고
    • Influence of the kinesin neck domain on dimerization and ATPase kinetics
    • Jiang, W., Stock, M. F., Li, X., and Hackney, D. D. (1997) Influence of the kinesin neck domain on dimerization and ATPase kinetics. J. Biol. Chem. 272, 7626-7632.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7626-7632
    • Jiang, W.1    Stock, M.F.2    Li, X.3    Hackney, D.D.4
  • 25
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure: Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils
    • Lau, S. Y. M., Taneja, A. K., and Hodges, R. S. (1984) Synthesis of a model protein of defined secondary and quaternary structure: Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils. J. Biol. Chem. 259, 13253-13261.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 26
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • Ma, Y. Z., and Taylor, E. W. (1997) Interacting head mechanism of microtubule-kinesin ATPase. J. Biol. Chem. 272, 724-730.
    • (1997) J. Biol. Chem. , vol.272 , pp. 724-730
    • Ma, Y.Z.1    Taylor, E.W.2
  • 27
    • 0031771084 scopus 로고    scopus 로고
    • The structural and mechanochemical cycle of kinesin
    • Mandelkow, E., and Johnson, K. A. (1998) The structural and mechanochemical cycle of kinesin. Trends Biochem. Sci. 23, 429-433.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 429-433
    • Mandelkow, E.1    Johnson, K.A.2
  • 28
    • 0029361842 scopus 로고
    • Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix
    • Monera, O. D., Sereda, T. J., Zhou, N. E., Kay, C. M., and Hodges, R. S. (1995) Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix. J. Pept. Sci. 1, 319-329.
    • (1995) J. Pept. Sci. , vol.1 , pp. 319-329
    • Monera, O.D.1    Sereda, T.J.2    Zhou, N.E.3    Kay, C.M.4    Hodges, R.S.5
  • 29
    • 0031016939 scopus 로고    scopus 로고
    • Identification of kinesin neck region as a stable alpha-helical coiled coil and its thermodynamic characterization
    • Morii, H., Takenawa, T., Arisaka, F., and Shimizu, T. (1997) Identification of kinesin neck region as a stable alpha-helical coiled coil and its thermodynamic characterization. Biochemistry 36, 1933-1942.
    • (1997) Biochemistry , vol.36 , pp. 1933-1942
    • Morii, H.1    Takenawa, T.2    Arisaka, F.3    Shimizu, T.4
  • 30
    • 0032548491 scopus 로고    scopus 로고
    • Pathway of ATP hydrolysis by monomeric and dimeric kinesin
    • Moyer, M. L., Gilbert, S. P., and Johnson, K. A. (1998) Pathway of ATP hydrolysis by monomeric and dimeric kinesin. Biochemistry 37, 800-813.
    • (1998) Biochemistry , vol.37 , pp. 800-813
    • Moyer, M.L.1    Gilbert, S.P.2    Johnson, K.A.3
  • 31
    • 0029009067 scopus 로고
    • The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding
    • Munoz, V., Blanco, F. J., and Serrano, L. (1995) The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding. Nature Struct. Biol. 2, 380-385.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 380-385
    • Munoz, V.1    Blanco, F.J.2    Serrano, L.3
  • 32
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-279.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-279
    • Pace, C.N.1
  • 34
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson, J. S., and Richardson, D. C. (1988) Amino acid preferences for specific locations at the ends of alpha helices. Science 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 35
    • 0032559824 scopus 로고    scopus 로고
    • Role of the kinesin neck region in processive microtubule-based motility
    • Romberg, L., Pierce, D. W., and Vale, R. D. (1998) Role of the kinesin neck region in processive microtubule-based motility. J. Cell Biol. 140, 1407-1416.
    • (1998) J. Cell Biol. , vol.140 , pp. 1407-1416
    • Romberg, L.1    Pierce, D.W.2    Vale, R.D.3
  • 37
    • 0035146785 scopus 로고    scopus 로고
    • Conformational changes during kinesin motility
    • Schief, W. R., and Howard, J. (2001) Conformational changes during kinesin motility. Curr. Opin. Cell Biol. 13, 19-28.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 19-28
    • Schief, W.R.1    Howard, J.2
  • 38
    • 0027986703 scopus 로고
    • Sequence determinants of the capping box, a stabilizing motif at the N-termini of alpha-helices
    • Seale, J. W., Srinivasan, R., and Rose, G. D. (1994) Sequence determinants of the capping box, a stabilizing motif at the N-termini of alpha-helices. Protein Sci. 3, 1741-1745.
    • (1994) Protein Sci. , vol.3 , pp. 1741-1745
    • Seale, J.W.1    Srinivasan, R.2    Rose, G.D.3
  • 39
    • 0034680321 scopus 로고    scopus 로고
    • Conformational preferences of a synthetic 30mer peptide from the interface between the neck and stalk regions of kinesin
    • Seeberger, C., Mandelkow, E., and Meyer, B. (2000) Conformational preferences of a synthetic 30mer peptide from the interface between the neck and stalk regions of kinesin. Biochemistry 39, 12558-12567.
    • (2000) Biochemistry , vol.39 , pp. 12558-12567
    • Seeberger, C.1    Mandelkow, E.2    Meyer, B.3
  • 40
    • 0027275192 scopus 로고
    • Effect of the alpha-amino group on peptide retention behaviour in reversed-phase chromatography. Determination of the pK(a) values of the alpha-amino group of 19 different N-terminal amino acid residues
    • Sereda, T. J., Mant, C. T., Quinn, A. M., and Hodges, R. S. (1993) Effect of the alpha-amino group on peptide retention behaviour in reversed-phase chromatography. Determination of the pK(a) values of the alpha-amino group of 19 different N-terminal amino acid residues. J. Chromatogr. 646, 17-30.
    • (1993) J. Chromatogr. , vol.646 , pp. 17-30
    • Sereda, T.J.1    Mant, C.T.2    Quinn, A.M.3    Hodges, R.S.4
  • 41
    • 0024972479 scopus 로고
    • Capping and alpha-helix stability
    • Serrano, L., and Fersht, A. R. (1989) Capping and alpha-helix stability. Nature 342, 296-299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 42
    • 0024550047 scopus 로고
    • Probing the determinants of protein folding and stability with amino acid substitutions
    • Shortel, D. (1989) Probing the determinants of protein folding and stability with amino acid substitutions. J. Biol. Chem. 264, 5315-5318.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5315-5318
    • Shortel, D.1
  • 45
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn, K. S., Ubersax, J. A., and Vale, R. D. (2000) Engineering the processive run length of the kinesin motor. J. Cell. Biol. 151, 1093-1100.
    • (2000) J. Cell. Biol. , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 46
    • 0034722388 scopus 로고    scopus 로고
    • Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change
    • Tomishige, M., and Vale, R. D. (2000) Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change. J. Cell Biol. 151, 1081-1092.
    • (2000) J. Cell Biol. , vol.151 , pp. 1081-1092
    • Tomishige, M.1    Vale, R.D.2
  • 47
    • 0030987241 scopus 로고    scopus 로고
    • Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides. Implications for motor activity
    • Tripet, B., Vale, R. D., and Hodges, R. S. (1997) Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides. Implications for motor activity. J. Biol. Chem. 272, 8946-8956.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8946-8956
    • Tripet, B.1    Vale, R.D.2    Hodges, R.S.3
  • 48
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y., and Yanagida, T. (1996) Direct observation of single kinesin molecules moving along microtubules. Nature 380, 451-453.
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 49
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R. D., and Milligan, R. A. (2000) The way things move: Looking under the hood of molecular motor proteins. Science 288, 88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 50
    • 0034303806 scopus 로고    scopus 로고
    • Walking on two heads: The many talents of kinesin
    • Woehlke, G., and Schliwa, M. (2000) Walking on two heads: The many talents of kinesin. Nature Rev. Mol. Cell. Biol. 1, 50-58.
    • (2000) Nature Rev. Mol. Cell. Biol. , vol.1 , pp. 50-58
    • Woehlke, G.1    Schliwa, M.2
  • 51
    • 0026609553 scopus 로고
    • The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions
    • Zhou, N. E., Zhu, B.-Y., Kay, C. M., and Hodges, R. S. (1992) The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions. Biopolymers 32, 419-426.
    • (1992) Biopolymers , vol.32 , pp. 419-426
    • Zhou, N.E.1    Zhu, B.-Y.2    Kay, C.M.3    Hodges, R.S.4
  • 52
    • 0027480940 scopus 로고
    • Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil
    • Zhou, N. E., Kay, C. M., and Hodges, R. S. (1993) Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil. Biochemistry 32, 3178-3187.
    • (1993) Biochemistry , vol.32 , pp. 3178-3187
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3


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