메뉴 건너뛰기




Volumn 246, Issue 2, 1997, Pages 380-387

Structural differences in the crossbridge head of temperature-associated myosin subfragment-1 isoforms from carp fast skeletal muscle

Author keywords

carp; Cyprinus carpio; Fast skeletal muscle; Myosin subfragment 1; Temperature acclimation

Indexed keywords

COMPLEMENTARY DNA; MYOSIN; MYOSIN HEAVY CHAIN;

EID: 0030909175     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-2-00380.x     Document Type: Article
Times cited : (69)

References (38)
  • 2
    • 0023729137 scopus 로고
    • Cross-linking of the skeletal myosin subfragment 1 heavy chain to the N-terminal actin segment of residues 40-113
    • Bertrand, R., Chaussepied, P., Kassab, R., Boyer, M., Roustan, C. & Benyamin, Y. (1988) Cross-linking of the skeletal myosin subfragment 1 heavy chain to the N-terminal actin segment of residues 40-113, Biochemistry 27, 5728-5736.
    • (1988) Biochemistry , vol.27 , pp. 5728-5736
    • Bertrand, R.1    Chaussepied, P.2    Kassab, R.3    Boyer, M.4    Roustan, C.5    Benyamin, Y.6
  • 3
    • 0028306266 scopus 로고
    • The covalent maleimidobenzoyl-actin-myosin head complex: Cross-linking of the 50 kDa heavy chain region to actin subdomain-2
    • Bertrand, R., Derancourt, J. & Kassah, R. (1994) The covalent maleimidobenzoyl-actin-myosin head complex: Cross-linking of the 50 kDa heavy chain region to actin subdomain-2, FEBS Lett. 345, 113-119.
    • (1994) FEBS Lett. , vol.345 , pp. 113-119
    • Bertrand, R.1    Derancourt, J.2    Kassah, R.3
  • 4
    • 0029935220 scopus 로고    scopus 로고
    • The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head
    • Bobkov, A. A., Bobkova, E. A., Lin, S. H. & Reisler, E. (1996) The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head, Proc. Natl Acad. Sci. USA 93, 2285-2289.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2285-2289
    • Bobkov, A.A.1    Bobkova, E.A.2    Lin, S.H.3    Reisler, E.4
  • 5
    • 0028351888 scopus 로고
    • Tropomyosin inhibits the glutaraldehyde-induced cross-link between the central 48-kDa fragment of myosin head and segment 48-67 in actin subdomain 2
    • Bonafé, N., Mathieu, M., Kassab, R. & Chaussepied, P. (1994) Tropomyosin inhibits the glutaraldehyde-induced cross-link between the central 48-kDa fragment of myosin head and segment 48-67 in actin subdomain 2, Biochemistry 33, 137-144.
    • (1994) Biochemistry , vol.33 , pp. 137-144
    • Bonafé, N.1    Mathieu, M.2    Kassab, R.3    Chaussepied, P.4
  • 6
    • 0029809252 scopus 로고    scopus 로고
    • Lower activation energy for sliding velocity of F-actin on a less thermostable isoform of carp myosin
    • Chaen, S., Nakaya, M. Quo, X. F. & Watabe, S. (1996) Lower activation energy for sliding velocity of F-actin on a less thermostable isoform of carp myosin, J. Biochem. (Tokyo) 120, 788-791.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 788-791
    • Chaen, S.1    Nakaya, M.2    Quo, X.F.3    Watabe, S.4
  • 7
    • 0342293921 scopus 로고
    • Modifying preselected sites on proteins: The stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site
    • Chaussepied, P. & Morales, M. F. (1988) Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site, Proc. Natl Acad. Sci. USA 85, 7471-7475.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7471-7475
    • Chaussepied, P.1    Morales, M.F.2
  • 8
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 9
    • 0029328581 scopus 로고
    • Small diameter white myotomal muscle fibres associated with growth hyperplasia in the carp (Cyprinus carpio) express a distinct myosin heavy chain gene
    • Ennion, S., Gauvry, L., Butterworth, P. & Goldspink, G. (1995) Small diameter white myotomal muscle fibres associated with growth hyperplasia in the carp (Cyprinus carpio) express a distinct myosin heavy chain gene, J. Exp. Biol. 198, 1603-1611.
    • (1995) J. Exp. Biol. , vol.198 , pp. 1603-1611
    • Ennion, S.1    Gauvry, L.2    Butterworth, P.3    Goldspink, G.4
  • 10
    • 0000193844 scopus 로고
    • Cruising speed of goldfish in relation to water temperature
    • Fry, F. E. J. & Hart, J. S. (1948) Cruising speed of goldfish in relation to water temperature, J. Fish. Res. Board Can. 7, 169-175.
    • (1948) J. Fish. Res. Board Can. , vol.7 , pp. 169-175
    • Fry, F.E.J.1    Hart, J.S.2
  • 11
    • 0029947401 scopus 로고    scopus 로고
    • The characterisation of the 5′ regulatory region of a temperature-induced myosin-heavy-chain gene associated with myotomal muscle growth in the carp
    • Gauvry, L., Ennion, S., Hansen, H., Butterworth, P. & Goldspink, G. (1996) The characterisation of the 5′ regulatory region of a temperature-induced myosin-heavy-chain gene associated with myotomal muscle growth in the carp, Eur. J. Biochem. 236, 887-894.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 887-894
    • Gauvry, L.1    Ennion, S.2    Hansen, H.3    Butterworth, P.4    Goldspink, G.5
  • 12
    • 0027993246 scopus 로고
    • Myosin subfragment-1 isoforms having different heavy chain structures from fast skeletal muscle of thermally acclimated carp
    • Guo, X. F., Nakaya, M. & Watabe, S. (1994) Myosin subfragment-1 isoforms having different heavy chain structures from fast skeletal muscle of thermally acclimated carp, J. Biochem. (Tokyo) 116, 728-735.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 728-735
    • Guo, X.F.1    Nakaya, M.2    Watabe, S.3
  • 13
    • 0000513081 scopus 로고
    • Consequences of thermal change on the myofibrillar ATPase of five freshwater teleosts
    • Heap, S. P., Watt, P. W. & Goldspink, G. (1985) Consequences of thermal change on the myofibrillar ATPase of five freshwater teleosts, J. Fish Biol. 26, 733-738.
    • (1985) J. Fish Biol. , vol.26 , pp. 733-738
    • Heap, S.P.1    Watt, P.W.2    Goldspink, G.3
  • 14
    • 0025113856 scopus 로고
    • Changes in carp myosin ATPase induced by temperature acclimation
    • Hwang, G. C., Watabe, S. & Hashimoto, K. (1990) Changes in carp myosin ATPase induced by temperature acclimation, J. Comp. Physiol. B 160, 233-239.
    • (1990) J. Comp. Physiol. B , vol.160 , pp. 233-239
    • Hwang, G.C.1    Watabe, S.2    Hashimoto, K.3
  • 15
    • 0000678368 scopus 로고
    • Changes of carp myosin subfragment-1 induced by temperature acclimation
    • Hwang, G. C., Ochiai, Y., Watabe, S. & Hashimoto, K. (1991) Changes of carp myosin subfragment-1 induced by temperature acclimation, J. Comp. Physiol. B 161, 141-146.
    • (1991) J. Comp. Physiol. B , vol.161 , pp. 141-146
    • Hwang, G.C.1    Ochiai, Y.2    Watabe, S.3    Hashimoto, K.4
  • 16
    • 0031019058 scopus 로고    scopus 로고
    • cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation
    • Imai, J., Hirayama, Y., Kikuchi, K., Kakinuma, M. & Watabe, S. (1997) cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation, J. Exp. Biol. 200, 27-34.
    • (1997) J. Exp. Biol. , vol.200 , pp. 27-34
    • Imai, J.1    Hirayama, Y.2    Kikuchi, K.3    Kakinuma, M.4    Watabe, S.5
  • 17
    • 0016424185 scopus 로고
    • 2+-activated myofibrillar ATPase activity induced by temperature acclimation
    • 2+-activated myofibrillar ATPase activity induced by temperature acclimation, FEBS Lett. 50, 293-295.
    • (1975) FEBS Lett. , vol.50 , pp. 293-295
    • Johnston, I.A.1    Davison, W.2    Goldspink, G.3
  • 18
    • 0027258646 scopus 로고
    • An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley, C. A., Takahashi, M., Yu, J. H. & Adelstein, R. S. (1993) An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature, J. Biol. Chem. 268, 12848-12854.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 19
    • 0028210495 scopus 로고
    • Kinetic mechanism of myofibril ATPase
    • Ma, Y. Z. & Taylor, E. W. (1994) Kinetic mechanism of myofibril ATPase, Biophys. J. 66, 1542-1553.
    • (1994) Biophys. J. , vol.66 , pp. 1542-1553
    • Ma, Y.Z.1    Taylor, E.W.2
  • 20
    • 0025826377 scopus 로고
    • The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1938-residue sequence of the heavy chain
    • Maita, T., Yajima, E., Nagata, S., Miyashita, T., Nakayama, S. & Matsuda, G. (1991) The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1938-residue sequence of the heavy chain, J. Biochem. (Tokyo) 110, 75-87.
    • (1991) J. Biochem. (Tokyo) , vol.110 , pp. 75-87
    • Maita, T.1    Yajima, E.2    Nagata, S.3    Miyashita, T.4    Nakayama, S.5    Matsuda, G.6
  • 21
    • 0028913571 scopus 로고
    • Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry
    • Nakaya, M., Watabe, S. & Ooi, T. (1995) Differences in the thermal stability of acclimation temperature-associated types of carp myosin and its rod on differential scanning calorimetry, Biochemistry 34, 3114-3120.
    • (1995) Biochemistry , vol.34 , pp. 3114-3120
    • Nakaya, M.1    Watabe, S.2    Ooi, T.3
  • 23
    • 0030061189 scopus 로고    scopus 로고
    • The structural basis of the myosin ATPase activity
    • Rayment, I. (1996) The structural basis of the myosin ATPase activity, J. Biol. Chem. 271, 15850-15853.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15850-15853
    • Rayment, I.1
  • 27
    • 0021368686 scopus 로고
    • Kinetics of the interaction between actin, ADP, and cardiac myosin-S1
    • Siemankowski, R. F. & White, H. D. (1984) Kinetics of the interaction between actin, ADP, and cardiac myosin-S1, J. Biol. Chem. 259, 5045-5053.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5045-5053
    • Siemankowski, R.F.1    White, H.D.2
  • 28
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J. A. (1994) How molecular motors work, Nature 372, 515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 29
    • 0020395203 scopus 로고
    • An actin-binding site on the 20 K fragment of myosin subfragment-1
    • Sutoh, K. (1982) An actin-binding site on the 20 K fragment of myosin subfragment-1, Biochemistry 21, 4800-4804.
    • (1982) Biochemistry , vol.21 , pp. 4800-4804
    • Sutoh, K.1
  • 30
    • 0020563473 scopus 로고
    • Mapping of actin-binding sites on the heavy chain of myosin subfragment 1
    • Sutoh, K. (1983) Mapping of actin-binding sites on the heavy chain of myosin subfragment 1, Biochemistry 22, 1579-1585.
    • (1983) Biochemistry , vol.22 , pp. 1579-1585
    • Sutoh, K.1
  • 31
    • 0025858239 scopus 로고
    • Site-directed mutations of Dictyostelium actin: Disruption of a negative charge cluster at the N-terminus
    • Sutoh, K. (1991) Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N-terminus, Proc. Natl Acad. Sci. USA 88, 7711-7714.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7711-7714
    • Sutoh, K.1
  • 32
    • 0027980111 scopus 로고
    • Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction
    • Sweeney, H. L., Straceski, A. J., Leinwand, L. A., Tikunov, B. A. & Faust, L. (1994) Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction, J. Biol. Chem. 269, 1603-1605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1603-1605
    • Sweeney, H.L.1    Straceski, A.J.2    Leinwand, L.A.3    Tikunov, B.A.4    Faust, L.5
  • 33
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • Uyeda, T. Q. P., Ruppel, K. M. & Spudich, J. A. (1994) Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin, Nature 368, 567-569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 35
    • 0027950192 scopus 로고
    • Carp express specific isoforms of the myosin cross-bridge head, subfragment-1, in association with cold and warm temperature acclimation
    • Watabe, S., Guo, X. F. & Hwang, G. C. (1994) Carp express specific isoforms of the myosin cross-bridge head, subfragment-1, in association with cold and warm temperature acclimation, J. Therm. Biol. 19, 261-268.
    • (1994) J. Therm. Biol. , vol.19 , pp. 261-268
    • Watabe, S.1    Guo, X.F.2    Hwang, G.C.3
  • 37
    • 0026101038 scopus 로고
    • Identification of the site important for the actin-activated MgATPase activity of myosin subfragment-1
    • Yamamoto, K. (1991) Identification of the site important for the actin-activated MgATPase activity of myosin subfragment-1, J. Mol. Biol. 217, 229-233.
    • (1991) J. Mol. Biol. , vol.217 , pp. 229-233
    • Yamamoto, K.1
  • 38
    • 0023661175 scopus 로고
    • Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin
    • Yanagisawa, M., Hamada, Y., Katsuragawa, Y., Imamura, M., Mikawa, T. & Masaki, T. (1987) Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin. J. Mol. Biol. 198, 143-157.
    • (1987) J. Mol. Biol. , vol.198 , pp. 143-157
    • Yanagisawa, M.1    Hamada, Y.2    Katsuragawa, Y.3    Imamura, M.4    Mikawa, T.5    Masaki, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.