메뉴 건너뛰기




Volumn 124, Issue 2-3, 1998, Pages 303-310

Nucleotide-dependent interaction of the N-terminal domain of MukB with microtubules

Author keywords

Chromosome partition; FtsZ; Kinesin; Motor; MukB; Tubulin

Indexed keywords

KINESIN; MICROTUBULE PROTEIN; MYOSIN;

EID: 0032465977     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.4056     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 0032481381 scopus 로고    scopus 로고
    • Proteolytic mapping of kinesin/ncd-microtubule interface: Nucleotide-dependent conformational changes in the loops L8 and L12
    • Alonso M. C., Damme J., Vandekerckhove J., Cross R. A. Proteolytic mapping of kinesin/ncd-microtubule interface: Nucleotide-dependent conformational changes in the loops L8 and L12. EMBO J. 17:1998;945-951.
    • (1998) EMBO J. , vol.17 , pp. 945-951
    • Alonso, M.C.1    Damme, J.2    Vandekerckhove, J.3    Cross, R.A.4
  • 2
    • 0030961727 scopus 로고    scopus 로고
    • Structures and dynamics of molecular motors
    • Amos L. A., Cross R. A. Structures and dynamics of molecular motors. Curr. Opin. Struct. Biol. 7:1997;239-246.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 239-246
    • Amos, L.A.1    Cross, R.A.2
  • 3
    • 0031042321 scopus 로고    scopus 로고
    • The structure of microtubule-motor complexes
    • Amos L. A., Hirose K. The structure of microtubule-motor complexes. Curr. Opin. Cell Biol. 9:1997;4-11.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 4-11
    • Amos, L.A.1    Hirose, K.2
  • 4
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division inEscherichia coli
    • Bi E., Lutkenhaus J. FtsZ ring structure associated with division inEscherichia coli. Nature. 354:1991;161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.1    Lutkenhaus, J.2
  • 5
    • 0028245510 scopus 로고
    • Yeast Kar3 is a minus-end directed microtubule motor protein that destabilises microtubules preferentially at the minus ends
    • Endow S. A., Kang S. J., Satterwhite L. L., Rose M. D., Skeen V. P., Salmon E. D. Yeast Kar3 is a minus-end directed microtubule motor protein that destabilises microtubules preferentially at the minus ends. EMBO J. 13:1994;2708-2713.
    • (1994) EMBO J. , vol.13 , pp. 2708-2713
    • Endow, S.A.1    Kang, S.J.2    Satterwhite, L.L.3    Rose, M.D.4    Skeen, V.P.5    Salmon, E.D.6
  • 6
    • 0028872562 scopus 로고
    • FtsZ, a prokaryotic homolog of tubulin
    • Erickson H. P. FtsZ, a prokaryotic homolog of tubulin. Cell. 80:1995;367-370.
    • (1995) Cell , vol.80 , pp. 367-370
    • Erickson, H.P.1
  • 7
    • 0030266954 scopus 로고    scopus 로고
    • Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to α/β and γ tubulin
    • Erickson H. P., Stoffler D. J. Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to α/β and γ tubulin. J. Cell Biol. 135:1996;5-8.
    • (1996) J. Cell Biol , vol.135 , pp. 5-8
    • Erickson, H.P.1    Stoffler, D.J.2
  • 8
    • 0345420017 scopus 로고
    • Expression, purification and characterisation of theDrosophilaEscherichia coli
    • Gilbert S. P., Johnston K. A. Expression, purification and characterisation of theDrosophilaEscherichia coli. Biochemistry. 32:1994;4677-4684.
    • (1994) Biochemistry , vol.32 , pp. 4677-4684
    • Gilbert, S.P.1    Johnston, K.A.2
  • 9
    • 0026705754 scopus 로고
    • Kinesin undergoes a 9 S to 6 S conformational transition
    • Hackney D. D., Levitt J. D., Suhan J. Kinesin undergoes a 9 S to 6 S conformational transition. J. Biol. Chem. 267:1992;8696-8701.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8696-8701
    • Hackney, D.D.1    Levitt, J.D.2    Suhan, J.3
  • 10
    • 0030930492 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: Structure, polarity and interaction with motor proteins
    • Hirose K., Amos W. B., Lockhart A., Cross R. A., Amos L. A. Three-dimensional cryoelectron microscopy of 16-protofilament microtubules: Structure, polarity and interaction with motor proteins. J. Struct. Biol. 118:1997;140-148.
    • (1997) J. Struct. Biol. , vol.118 , pp. 140-148
    • Hirose, K.1    Amos, W.B.2    Lockhart, A.3    Cross, R.A.4    Amos, L.A.5
  • 12
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull F. J., Sablin E. P., Lau R., Fletterick R. J., Vale R. D. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature. 380:1996;550-555.
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 13
    • 0022412823 scopus 로고
    • Attachment of transported vesicles to microtubules in axoplasm is facilitated by AMPPNP
    • Lasek R. J., Brady S. T. Attachment of transported vesicles to microtubules in axoplasm is facilitated by AMPPNP. Nature. 316:1985;645-647.
    • (1985) Nature , vol.316 , pp. 645-647
    • Lasek, R.J.1    Brady, S.T.2
  • 14
    • 0031973946 scopus 로고    scopus 로고
    • Cell cycle: The bacterial approach to coordination
    • Levin P. A., Grossman A. D. Cell cycle: The bacterial approach to coordination. Curr. Biol. 8:1998;R28-R31.
    • (1998) Curr. Biol. , vol.8
    • Levin, P.A.1    Grossman, A.D.2
  • 15
    • 0026539415 scopus 로고
    • Suppression of a myosin defect by a kinesin-related gene
    • Lillie S. H., Brown S. S. Suppression of a myosin defect by a kinesin-related gene. Nature. 356:1992;358-360.
    • (1992) Nature , vol.356 , pp. 358-360
    • Lillie, S.H.1    Brown, S.S.2
  • 16
    • 0028040295 scopus 로고
    • Origins of reversed directionality in the ncd molecular motor
    • Lockhart A., Cross R. A. Origins of reversed directionality in the ncd molecular motor. EMBO J. 13:1994;751-757.
    • (1994) EMBO J. , vol.13 , pp. 751-757
    • Lockhart, A.1    Cross, R.A.2
  • 17
    • 0030044339 scopus 로고    scopus 로고
    • Kinetics and motility of the Eg5 microtubule motor
    • Lockhart A., Cross R. A. Kinetics and motility of the Eg5 microtubule motor. Biochemistry. 35:1996;2365-2373.
    • (1996) Biochemistry , vol.35 , pp. 2365-2373
    • Lockhart, A.1    Cross, R.A.2
  • 18
    • 0032479196 scopus 로고    scopus 로고
    • Interaction of the N-terminal domain of MukB with the bacterial tubulin homologue FtsZ
    • Lockhart A., Kendrick-Jones J. Interaction of the N-terminal domain of MukB with the bacterial tubulin homologue FtsZ. FEBS Letts. 430:1998;278-282.
    • (1998) FEBS Letts. , vol.430 , pp. 278-282
    • Lockhart, A.1    Kendrick-Jones, J.2
  • 19
    • 0029012977 scopus 로고
    • Kinesin and ncd bind through a single head to microtubules and compete for a shared Mt binding site
    • Lockhart A., Crevel I. M.-T. C., Cross R. A. Kinesin and ncd bind through a single head to microtubules and compete for a shared Mt binding site. J. Mol. Biol. 249:1995;763-771.
    • (1995) J. Mol. Biol. , vol.249 , pp. 763-771
    • Lockhart, A.1    Crevel I.M.-T., C.2    Cross, R.A.3
  • 20
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Lowe J., Amos L. A. Crystal structure of the bacterial cell-division protein FtsZ. Nature. 391:1998;203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 21
    • 0029851154 scopus 로고    scopus 로고
    • Colocalisation of the cell division proteins FtsZ and FtsA to cytoskeletal structures in livingEscherichia coli
    • Ma X., Ehrhard D. W., Margolin W. Colocalisation of the cell division proteins FtsZ and FtsA to cytoskeletal structures in livingEscherichia coli. Proc. Natl. Acad. Sci. USA. 93:1996;12998-13003.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhard, D.W.2    Margolin, W.3
  • 22
    • 0031022509 scopus 로고    scopus 로고
    • Kinetic mechanism of a monomeric kinesin construct
    • Ma Y-Z., Taylor E. W. Kinetic mechanism of a monomeric kinesin construct. J. Biol. Chem. 272:1997;717-723.
    • (1997) J. Biol. Chem. , vol.272 , pp. 717-723
    • Ma, Y-Z.1    Taylor, E.W.2
  • 23
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T., Kirschner M. Dynamic instability of microtubule growth. Nature. 312:1984;237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 24
    • 0028274791 scopus 로고
    • Guanine nucleotide-dependent assembly of FtsZ into filaments
    • Mukherjee A., Lutkenhaus J. Guanine nucleotide-dependent assembly of FtsZ into filaments. J. Bacteriol. 176:1994;2754-2758.
    • (1994) J. Bacteriol. , vol.176 , pp. 2754-2758
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 25
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • Mukherjee A., Lutkenhaus J. Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 17:1998;462-469.
    • (1998) EMBO J. , vol.17 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 28
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin heterodimer by electron microscopy
    • Nogales E., Wolf S. G., Downing K. Structure of the αβ tubulin heterodimer by electron microscopy. Nature. 391:1998;199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.3
  • 31
    • 0028246571 scopus 로고
    • Bacterial chromosome segregation
    • Rothfield L. Bacterial chromosome segregation. Cell. 77:1994;963-966.
    • (1994) Cell , vol.77 , pp. 963-966
    • Rothfield, L.1
  • 32
    • 0029878485 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the kinesin-related motor ncd
    • Sablin E. P., Kull F. J., Cooke R., Vale R. D., Fletterick R. J. Crystal structure of the motor domain of the kinesin-related motor ncd. Nature. 380:1996;555-559.
    • (1996) Nature , vol.380 , pp. 555-559
    • Sablin, E.P.1    Kull, F.J.2    Cooke, R.3    Vale, R.D.4    Fletterick, R.J.5
  • 35
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to b-tubilin and decorates microtubules with a B surface lattice
    • Song Y. H., Mandelkow E. Recombinant kinesin motor domain binds to b-tubilin and decorates microtubules with a B surface lattice. Proc. Natl. Acad. Sci. USA. 90:1993;1671-1675.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1671-1675
    • Song, Y.H.1    Mandelkow, E.2
  • 36
    • 0027279053 scopus 로고
    • Direction of microtubule movement is an intrinsic property of the motor domains of the kinesin heavy chain andDrosophila
    • Stewart R. J., Thaler J. P., Goldstein L. S. Direction of microtubule movement is an intrinsic property of the motor domains of the kinesin heavy chain andDrosophila. Proc. Natl. Acad. Sci. USA. 90:1993;5209-5213.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5209-5213
    • Stewart, R.J.1    Thaler, J.P.2    Goldstein, L.S.3
  • 37
    • 0019917760 scopus 로고
    • ATP-induced reversible change in the conformation of the chicken gizzard myosin and heavy meromyosin
    • Suzuki H., Kamata T., Ohnishi H., Watanabe S. ATP-induced reversible change in the conformation of the chicken gizzard myosin and heavy meromyosin. J. Biochem. 91:1982;1699-1705.
    • (1982) J. Biochem. , vol.91 , pp. 1699-1705
    • Suzuki, H.1    Kamata, T.2    Ohnishi, H.3    Watanabe, S.4
  • 38
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 39
    • 0029055373 scopus 로고
    • Ncd and kinesin motor domains interact with both α and β tubulin
    • Walker R. A. Ncd and kinesin motor domains interact with both α and β tubulin. Proc. Natl. Acad. Sci. USA. 92:1995;5960-5964.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5960-5964
    • Walker, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.