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Volumn 77, Issue 3, 1999, Pages 1518-1527

Dynein-ADP as a force-generating intermediate revealed by a rapid reactivation of flagellar axoneme

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 0032856096     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76999-7     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 0024513711 scopus 로고
    • Direct measurements of sliding between outer doublet microtubules in swimming sperm flagella
    • Brokaw, C. J. 1989. Direct measurements of sliding between outer doublet microtubules in swimming sperm flagella. Science. 243:1593-1596.
    • (1989) Science. , vol.243 , pp. 1593-1596
    • Brokaw, C.J.1
  • 2
    • 0014294669 scopus 로고
    • Mechanochemical coupling in flagella. I. Movement-dependent dephosphorylation of ATP in glycerinated spermatozoa
    • Brokaw, C. J., and B. Benedict. 1968. Mechanochemical coupling in flagella. I. Movement-dependent dephosphorylation of ATP in glycerinated spermatozoa. Arch. Biochem. Biophys. 125:770-778.
    • (1968) Arch. Biochem. Biophys. , vol.125 , pp. 770-778
    • Brokaw, C.J.1    Benedict, B.2
  • 3
    • 0029068861 scopus 로고
    • Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella
    • Burgess, S. A. 1995. Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella. J. Mol. Biol 250:52-63.
    • (1995) J. Mol. Biol , vol.250 , pp. 52-63
    • Burgess, S.A.1
  • 4
    • 0020348926 scopus 로고
    • Sliding and bending in sea urchin sperm flagella
    • Prokaryotic and Eukaryotic Flagella. W. B. Amos and J. G. Duckette, eds. Cambridge University Press, Cambridge
    • Gibbons, I. R. 1982. Sliding and bending in sea urchin sperm flagella. In Symp. Soc. Exp. Biol. vol. 35, Prokaryotic and Eukaryotic Flagella. W. B. Amos and J. G. Duckette, eds. Cambridge University Press, Cambridge. 225-287.
    • (1982) Symp. Soc. Exp. Biol. , vol.35 , pp. 225-287
    • Gibbons, I.R.1
  • 5
    • 0015372444 scopus 로고
    • Flagellar movement and adenosine triphosphatase activity in sea-urchin sperm extracted with Triton X-100
    • Gibbons, B. H., and I. R. Gibbons. 1972. Flagellar movement and adenosine triphosphatase activity in sea-urchin sperm extracted with Triton X-100. J. Cell Biol. 54:78-97.
    • (1972) J. Cell Biol. , vol.54 , pp. 78-97
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 6
    • 0016265494 scopus 로고
    • Properties of flagellai "rigor waves" formed by abrupt removal of adenosine triphosphate from actively swimming sea urchin sperm
    • Gibbons, B. H., and I. R. Gibbons. 1974. Properties of flagellai "rigor waves" formed by abrupt removal of adenosine triphosphate from actively swimming sea urchin sperm. J, Cell Biol. 63:970-985.
    • (1974) J, Cell Biol. , vol.63 , pp. 970-985
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 8
    • 85005068023 scopus 로고
    • Acetate anions stabilize the latency of dynein 1 ATPase and increase the velocity of tubule sliding in reactivated sperm flagella
    • Gibbons, I. R., J. A. Evans, and B. H. Gibbons. 1982. Acetate anions stabilize the latency of dynein 1 ATPase and increase the velocity of tubule sliding in reactivated sperm flagella. Cell Motil. (suppl.) 1:181-184.
    • (1982) Cell Motil. (Suppl.) , vol.1 , pp. 181-184
    • Gibbons, I.R.1    Evans, J.A.2    Gibbons, B.H.3
  • 9
    • 0026425402 scopus 로고
    • Multiple nucleotide-binding sites in the sequence of dynein β heavy chain
    • Gibbons, I. R., B. H. Gibbons, G. Mocz, and D. J. Asai. 1991. Multiple nucleotide-binding sites in the sequence of dynein β heavy chain. Nature. 352:640-643.
    • (1991) Nature. , vol.352 , pp. 640-643
    • Gibbons, I.R.1    Gibbons, B.H.2    Mocz, G.3    Asai, D.J.4
  • 10
    • 0020438546 scopus 로고
    • Relaxation of muscle fibres by photolysis of caged ATP
    • Goldman, Y. E., M. G. Hibberd, J. A. McCray, and D. R. Trentham. 1982. Relaxation of muscle fibres by photolysis of caged ATP. Nature. 300: 701-705.
    • (1982) Nature. , vol.300 , pp. 701-705
    • Goldman, Y.E.1    Hibberd, M.G.2    McCray, J.A.3    Trentham, D.R.4
  • 11
    • 0020410980 scopus 로고
    • Substructure of the outer dynein arm
    • Goodenough, U. W., and J. E. Heuser. 1982. Substructure of the outer dynein arm. J. Cell Biol. 95:798-815.
    • (1982) J. Cell Biol. , vol.95 , pp. 798-815
    • Goodenough, U.W.1    Heuser, J.E.2
  • 13
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd, M. G., J. A. Dantzig, D. R. Trentham, and Y. E. Goldman. 1985. Phosphate release and force generation in skeletal muscle fibers. Science. 228:1317-1319.
    • (1985) Science. , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Trentham, D.R.3    Goldman, Y.E.4
  • 14
    • 0030935659 scopus 로고    scopus 로고
    • Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP
    • Higuchi, H., E. Muto, Y. Inoue, and T. Yanagida. 1997. Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP. Proc. Natl. Acad. Sei. USA. 94:4395-4400.
    • (1997) Proc. Natl. Acad. Sei. USA. , vol.94 , pp. 4395-4400
    • Higuchi, H.1    Muto, E.2    Inoue, Y.3    Yanagida, T.4
  • 15
    • 0024320810 scopus 로고
    • ADP release is rate limiting in steady-state turnover by the dynein adenosinetriphosphatase
    • Holzbaur, E. L., and K. A. Johnson. 1989a. ADP release is rate limiting in steady-state turnover by the dynein adenosinetriphosphatase. Biochemistry. 28:5577-5585.
    • (1989) Biochemistry. , vol.28 , pp. 5577-5585
    • Holzbaur, E.L.1    Johnson, K.A.2
  • 16
    • 0024445251 scopus 로고
    • Microtubules accelerate ADP release by dynein
    • Holzbaur, E. L., and K. A. Johnson. 1989b. Microtubules accelerate ADP release by dynein. Biochemistry. 28:7010-7016.
    • (1989) Biochemistry. , vol.28 , pp. 7010-7016
    • Holzbaur, E.L.1    Johnson, K.A.2
  • 17
    • 0024746385 scopus 로고
    • Anthraniloyl ATP, a fluorescent analog of ATP, as a substrate for dynein ATPase and flagellar motility
    • Inaba, K., M. Okuno, and H. Mohri. 1989. Anthraniloyl ATP, a fluorescent analog of ATP, as a substrate for dynein ATPase and flagellar motility. Arch. Biochem. Biophys. 274:209-215.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 209-215
    • Inaba, K.1    Okuno, M.2    Mohri, H.3
  • 18
    • 0024336008 scopus 로고
    • Dynamic conformational changes of 21S dynein ATPase coupled with ATP hydrolysis revealed by proteolytic digestion
    • Inaba, K., and H. Mohri. 1989. Dynamic conformational changes of 21S dynein ATPase coupled with ATP hydrolysis revealed by proteolytic digestion. J. Biol. Chem. 264:8384-8388.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8384-8388
    • Inaba, K.1    Mohri, H.2
  • 19
    • 0021070504 scopus 로고
    • The pathway of ATP hydrolysis by dynein: Kinetics of a presteady state phosphate burst
    • Johnson, K. A. 1983. The pathway of ATP hydrolysis by dynein: kinetics of a presteady state phosphate burst. J. Biol. Chem. 258:13825-13832.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13825-13832
    • Johnson, K.A.1
  • 20
    • 0027097082 scopus 로고
    • Translocation and rotation of microrubules caused by multiple species of Chlamydomonas inner-arm dynein
    • Kagami, O., and R. Kamiya. 1992. Translocation and rotation of microrubules caused by multiple species of Chlamydomonas inner-arm dynein. J. Cell Sei. 103:653-664.
    • (1992) J. Cell Sei. , vol.103 , pp. 653-664
    • Kagami, O.1    Kamiya, R.2
  • 21
    • 0001347489 scopus 로고
    • Direct measurement of nanometric displacement under an optical microscope
    • Kamimura, S. 1987. Direct measurement of nanometric displacement under an optical microscope. Applied Optics. 26:3425-3427.
    • (1987) Applied Optics. , vol.26 , pp. 3425-3427
    • Kamimura, S.1
  • 22
    • 0019881875 scopus 로고
    • Direct measurement of the force of microtubule sliding in flagella
    • Kamimura, S., and K. Takahashi. 1981. Direct measurement of the force of microtubule sliding in flagella. Nature. 293:566-568.
    • (1981) Nature. , vol.293 , pp. 566-568
    • Kamimura, S.1    Takahashi, K.2
  • 23
    • 0024322107 scopus 로고
    • High-frequency nanometre-scale vibration in 'quiescent' flagellar axonemes
    • Kamimura, S., and R. Kamiya. 1989. High-frequency nanometre-scale vibration in 'quiescent' flagellar axonemes. Nature. 340:476-478.
    • (1989) Nature. , vol.340 , pp. 476-478
    • Kamimura, S.1    Kamiya, R.2
  • 24
    • 0026507051 scopus 로고
    • High-frequency vibration in flagellar axonemes with amplitudes reflect the size of tubulin
    • Kamimura, S., and R. Kamiya. 1992. High-frequency vibration in flagellar axonemes with amplitudes reflect the size of tubulin. J. Cell Biol. 116:1443-1454.
    • (1992) J. Cell Biol. , vol.116 , pp. 1443-1454
    • Kamimura, S.1    Kamiya, R.2
  • 25
    • 0017867017 scopus 로고
    • Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: Utilization by the Na: K pump of human red blood cell ghosts
    • Kaplan, J. H., B. Forbush, III, and J. H. Huffman. 1978. Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: Utilization by the Na: K pump of human red blood cell ghosts. Biochemistry. 17:1929-1935.
    • (1978) Biochemistry. , vol.17 , pp. 1929-1935
    • Kaplan, J.H.1    Forbush III, B.2    Huffman, J.H.3
  • 26
    • 33646959310 scopus 로고
    • Inhibition of dynein ATPase by vanadate and its possible use as a probe for the role of dynein in cytoplasmic motility
    • Kobayashi, T., T. Martensen, J. Nath, and M. Ravin. 1978. Inhibition of dynein ATPase by vanadate and its possible use as a probe for the role of dynein in cytoplasmic motility. Biochem. Biophys. Acta. 16:146-154.
    • (1978) Biochem. Biophys. Acta. , vol.16 , pp. 146-154
    • Kobayashi, T.1    Martensen, T.2    Nath, J.3    Ravin, M.4
  • 27
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn, R. W., and E. W. Taylor. 1971. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 10:4617-4624.
    • (1971) Biochemistry. , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 28
    • 0001346971 scopus 로고
    • A new approach to time-resolved studies of ATP-requiring biological systems: Laser flash photolysis of caged ATP
    • McCray, J. A., L. Herbette, T. Kihara, and D. R. Trentham. 1980. A new approach to time-resolved studies of ATP-requiring biological systems: laser flash photolysis of caged ATP. Proc. Nail. Acad. Sei. USA. 77: 7237-7241.
    • (1980) Proc. Nail. Acad. Sei. USA. , vol.77 , pp. 7237-7241
    • McCray, J.A.1    Herbette, L.2    Kihara, T.3    Trentham, D.R.4
  • 29
    • 0032493320 scopus 로고    scopus 로고
    • Probing the nucleotide binding sites of axonemal dynein with the fluorescent nucleotide analogue 2′(3′)-O-(-N-Methylanthraniloyl)-adenosine 5′-triphosphate
    • Mocz, G., M. K. Helms, D. M. Jameson, and I. R. Gibbons. 1998. Probing the nucleotide binding sites of axonemal dynein with the fluorescent nucleotide analogue 2′(3′)-O-(-N-Methylanthraniloyl)-adenosine 5′-triphosphate. Biochemistry. 37:9862-9869.
    • (1998) Biochemistry. , vol.37 , pp. 9862-9869
    • Mocz, G.1    Helms, M.K.2    Jameson, D.M.3    Gibbons, I.R.4
  • 30
    • 0026425498 scopus 로고
    • Four ATP-binding sites in the midregion of the β heavy chain of dynein
    • Ogawa, K. 1991. Four ATP-binding sites in the midregion of the β heavy chain of dynein. Nature. 352:643-645.
    • (1991) Nature. , vol.352 , pp. 643-645
    • Ogawa, K.1
  • 31
    • 0023678895 scopus 로고
    • The force-velocity relationship for microtubule sliding in demembranated sperm flagella of sea urchin sperm
    • Oiwa, K., and K. Takahashi. 1988. The force-velocity relationship for microtubule sliding in demembranated sperm flagella of sea urchin sperm. Cell Struct. Func. 13:193-205.
    • (1988) Cell Struct. Func. , vol.13 , pp. 193-205
    • Oiwa, K.1    Takahashi, K.2
  • 32
    • 0018942981 scopus 로고
    • Inhibition and relaxation of sea urchin sperm flagella by vanadate
    • Okuno, M. 1980. Inhibition and relaxation of sea urchin sperm flagella by vanadate. J. Cell'Biol. 85:712-725.
    • (1980) J. Cell'Biol. , vol.85 , pp. 712-725
    • Okuno, M.1
  • 33
    • 0027086965 scopus 로고
    • Sea urchin sperm axonemal motion supported by fluorescent, ribose-modified analogues of ATP
    • Omoto, C. K. 1992. Sea urchin sperm axonemal motion supported by fluorescent, ribose-modified analogues of ATP. J. Musc. Res. Cell Motil. 13:635-639.
    • (1992) J. Musc. Res. Cell Motil. , vol.13 , pp. 635-639
    • Omoto, C.K.1
  • 34
    • 0022525167 scopus 로고
    • Activation of the dynein adenosine triphosphatase by microtubules
    • Omoto, C. K., and K. A. Johnson. 1986. Activation of the dynein adenosine triphosphatase by microtubules. Biochemistry. 25:419-427.
    • (1986) Biochemistry. , vol.25 , pp. 419-427
    • Omoto, C.K.1    Johnson, K.A.2
  • 35
    • 0021112029 scopus 로고
    • Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex
    • Porter, M. E., and K. A. Johnson. 1983. Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex. J. Biol. Chem. 258:6582-6587.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6582-6587
    • Porter, M.E.1    Johnson, K.A.2
  • 36
    • 0018428390 scopus 로고
    • Study of the mechanism of vanadate inhibition of the dynein cross-bridge cycle in sea urchin sperm flagella
    • Sale, W. S., and I. R. Gibbons. 1979. Study of the mechanism of vanadate inhibition of the dynein cross-bridge cycle in sea urchin sperm flagella. J. Cell Biol. 82:291-298.
    • (1979) J. Cell Biol. , vol.82 , pp. 291-298
    • Sale, W.S.1    Gibbons, I.R.2
  • 37
    • 0019885880 scopus 로고
    • Steady-state kinetic study of vanadate-induced inhibition of ciliary dynein adenosinetriphosphatase activity from Tetrahymena
    • Shimizu, T. 1981. Steady-state kinetic study of vanadate-induced inhibition of ciliary dynein adenosinetriphosphatase activity from Tetrahymena. Biochemistry. 20:4347-4354.
    • (1981) Biochemistry. , vol.20 , pp. 4347-4354
    • Shimizu, T.1
  • 38
    • 0021020391 scopus 로고
    • Presteady state kinetic analysis of vanadate-induced inhibition of the dynein ATPase
    • Shimizu, T., and K. A. Johnson. 1983. Presteady state kinetic analysis of vanadate-induced inhibition of the dynein ATPase. J. Biol. Chem. 258: 13833-13840.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13833-13840
    • Shimizu, T.1    Johnson, K.A.2
  • 39
    • 0024434666 scopus 로고
    • Activation of the dynein adenosine triphosphatase by cross-linking to microtubules
    • Shimizu, T., S.-P. Marchese-Rogana, and K. A. Johnson. 1989. Activation of the dynein adenosine triphosphatase by cross-linking to microtubules. Biochemistry. 28:7016-7021.
    • (1989) Biochemistry. , vol.28 , pp. 7016-7021
    • Shimizu, T.1    Marchese-Rogana, S.-P.2    Johnson, K.A.3
  • 40
    • 0028917181 scopus 로고
    • Cyclical bending movements induced locally by successive iontophoretic application of ATP to an elastase-treated flagellar axoneme
    • Shingyoji, C., and K. Takahashi. 1995. Cyclical bending movements induced locally by successive iontophoretic application of ATP to an elastase-treated flagellar axoneme. J. Cell Sei. 108:1359-1369.
    • (1995) J. Cell Sei. , vol.108 , pp. 1359-1369
    • Shingyoji, C.1    Takahashi, K.2
  • 41
    • 0015188644 scopus 로고
    • Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm
    • Summers, K. E., and I. R. Gibbons. 1971. Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm. Proc. Natl. Acad. Sei. USA. 68:3092-3096.
    • (1971) Proc. Natl. Acad. Sei. USA. , vol.68 , pp. 3092-3096
    • Summers, K.E.1    Gibbons, I.R.2
  • 42
    • 0020350067 scopus 로고
    • Microtubule sliding in reactivated flagella
    • Prokaryotic and Eukaryotic Flagella. W. B. Amos and J. G. Duckette, eds. Cambridge University Press, Cambridge
    • Takahashi, K., C. Shingyoji, and S. Kamimura. 1982. Microtubule sliding in reactivated flagella. In Symp. Soc. Exp. Biol. vol. 35, Prokaryotic and Eukaryotic Flagella. W. B. Amos and J. G. Duckette, eds. Cambridge University Press, Cambridge. 159-177.
    • (1982) Symp. Soc. Exp. Biol. , vol.35 , pp. 159-177
    • Takahashi, K.1    Shingyoji, C.2    Kamimura, S.3
  • 43
    • 0032079197 scopus 로고    scopus 로고
    • Reactivation of sea-urchin sperm flagella induced by rapid photolysis of caged ATP
    • Tani, T., and S. Kamimura. 1998. Reactivation of sea-urchin sperm flagella induced by rapid photolysis of caged ATP. J. Exp. Biol. 201:1493-1503.
    • (1998) J. Exp. Biol. , vol.201 , pp. 1493-1503
    • Tani, T.1    Kamimura, S.2
  • 44
    • 0028941575 scopus 로고
    • Inhibition of unloaded shortening velocity in permeabilized muscle fibres by caged ATP compounds
    • Thirlwell, H., J. A. Sleep, and M. A. Ferenczi. 1995. Inhibition of unloaded shortening velocity in permeabilized muscle fibres by caged ATP compounds. J. Muscle Res. Cell Motil. 16:131-137.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 131-137
    • Thirlwell, H.1    Sleep, J.A.2    Ferenczi, M.A.3
  • 45
    • 0020518435 scopus 로고
    • ATP-dependent changes of the outer dynein arm in Tetrahymena cilia: A freeze-etch replica study
    • Tsukita, S., S. Tuskita, J. Usukura, and H. Ishikawa. 1983. ATP-dependent changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study. J. Cell Biol. 96:1480-1485.
    • (1983) J. Cell Biol. , vol.96 , pp. 1480-1485
    • Tsukita, S.1    Tuskita, S.2    Usukura, J.3    Ishikawa, H.4
  • 46
    • 0022294771 scopus 로고
    • Different axoplasmic proteins generate movement in opposite directions along microtubules in vitro
    • Vale, R. D., B. J. Schnapp, T. Mitchison, E. Steuer, T. S. Reese, and M. P. Sheetz. 1985. Different axoplasmic proteins generate movement in opposite directions along microtubules in vitro. Cell. 43:623-632.
    • (1985) Cell. , vol.43 , pp. 623-632
    • Vale, R.D.1    Schnapp, B.J.2    Mitchison, T.3    Steuer, E.4    Reese, T.S.5    Sheetz, M.P.6
  • 47
    • 0024805563 scopus 로고
    • One dimensional diffusion of microtubules bound to flagellar dynein
    • Vale, R. D., D. R. Soll, and I. R. Gibbons. 1989. One dimensional diffusion of microtubules bound to flagellar dynein. Cell. 59:915-925.
    • (1989) Cell. , vol.59 , pp. 915-925
    • Vale, R.D.1    Soll, D.R.2    Gibbons, I.R.3
  • 49
    • 0027964583 scopus 로고
    • Nanometer scale vibration in mutant axonemes of Chlamydomonas
    • Yagi, T., S. Kamimura, and Y. Kamiya. 1994. Nanometer scale vibration in mutant axonemes of Chlamydomonas. Cell Motil. Cytoskeleton. 29: 177-185.
    • (1994) Cell Motil. Cytoskeleton. , vol.29 , pp. 177-185
    • Yagi, T.1    Kamimura, S.2    Kamiya, Y.3
  • 50
    • 0019231308 scopus 로고
    • Sliding velocity between outer doublet microtubules of sea-urchin sperm axonemes
    • Yano, Y., and Miki-Noumura 1980. Sliding velocity between outer doublet microtubules of sea-urchin sperm axonemes. J. Cell Sei. 44:169-186.
    • (1980) J. Cell Sei. , vol.44 , pp. 169-186
    • Yano, Y.1    Miki-Noumura2
  • 51
    • 0001521636 scopus 로고
    • Force exerted by a single cilium of Mytilus edulis
    • Yoneda, M. 1960. Force exerted by a single cilium of Mytilus edulis. Int. J. Exp. Biol. 37:461-468.
    • (1960) Int. J. Exp. Biol. , vol.37 , pp. 461-468
    • Yoneda, M.1


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