메뉴 건너뛰기




Volumn 16, Issue 6, 2007, Pages 1017-1023

Single molecule analyses of the conformational substates of calmodulin bound to the phosphorylase kinase complex

Author keywords

; Ca2+; CaM; Conformational substates; Distance distribution; Phosphorylase kinase; spFRET

Indexed keywords

CALCIUM; CALMODULIN; PHOSPHORYLASE KINASE;

EID: 34249790883     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062747407     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 1642497604 scopus 로고    scopus 로고
    • Fluorescence labeling, purification, and immobilization of a double cysteine mutant calmodulin fusion protein for single-molecule experiments
    • Allen, M.W., Urbauer, R.J., Zaidi, A., Williams, T.D., Urbauer, J.L., and Johnson, C.K. 2004. Fluorescence labeling, purification, and immobilization of a double cysteine mutant calmodulin fusion protein for single-molecule experiments. Anal. Biochem. 325: 273-284.
    • (2004) Anal. Biochem , vol.325 , pp. 273-284
    • Allen, M.W.1    Urbauer, R.J.2    Zaidi, A.3    Williams, T.D.4    Urbauer, J.L.5    Johnson, C.K.6
  • 2
    • 0032055052 scopus 로고    scopus 로고
    • Effector-sensitive cross-linking of phosphorylase b kinase by the novel cross-linker 4-phenyl-1,2,4-triazoline-3,5-dione
    • Ayers, N.A., Nadeau, O.W., Read, M.W., Ray, P., and Carlson, G.M. 1998. Effector-sensitive cross-linking of phosphorylase b kinase by the novel cross-linker 4-phenyl-1,2,4-triazoline-3,5-dione. Biochem. J. 331: 137-141.
    • (1998) Biochem. J , vol.331 , pp. 137-141
    • Ayers, N.A.1    Nadeau, O.W.2    Read, M.W.3    Ray, P.4    Carlson, G.M.5
  • 3
    • 0034789588 scopus 로고    scopus 로고
    • Analysis of slow interdomain motion of macromolecules using NMR relaxation data
    • Baber, J.L., Szabo, A., and Tjandra, N. 2001. Analysis of slow interdomain motion of macromolecules using NMR relaxation data. J. Am. Chem. Soc. 123: 3953-3959.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 3953-3959
    • Baber, J.L.1    Szabo, A.2    Tjandra, N.3
  • 4
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • Babu, Y.S., Bugg, C.E., and Cook, W.J. 1988. Structure of calmodulin refined at 2.2 A resolution. J. Mol. Biol. 204: 191-204.
    • (1988) J. Mol. Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 5
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • Barbato, G., Ikura, M., Kay, L.E., Pastor, R.W., and Bax, A. 1992. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31: 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 7
    • 0033567657 scopus 로고    scopus 로고
    • Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure
    • Brushia, R.J. and Walsh, D.A. 1999. Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure. Front. Biosci. 4: D618-D641.
    • (1999) Front. Biosci , vol.4
    • Brushia, R.J.1    Walsh, D.A.2
  • 8
    • 0021100478 scopus 로고
    • Free energy coupling in the interactions between Ca2+, calmodulin, and phosphorylase kinase
    • Burger, D., Stein, E.A., and Cox, J.A. 1983. Free energy coupling in the interactions between Ca2+, calmodulin, and phosphorylase kinase. J. Biol. Chem. 258: 14733-14739.
    • (1983) J. Biol. Chem , vol.258 , pp. 14733-14739
    • Burger, D.1    Stein, E.A.2    Cox, J.A.3
  • 9
    • 0043194166 scopus 로고    scopus 로고
    • Temperature dependence of domain motions of calmodulin probed by NMR relaxation at multiple fields
    • Chang, S.L., Szabo, A., and Tjandra, N. 2003. Temperature dependence of domain motions of calmodulin probed by NMR relaxation at multiple fields. J. Am. Chem. Soc. 125: 11379-11384.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 11379-11384
    • Chang, S.L.1    Szabo, A.2    Tjandra, N.3
  • 10
    • 0018198417 scopus 로고
    • Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase
    • Cohen, P., Burchell, A., Foulkes, J.G., and Cohen, P.T. 1978. Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett. 92: 287-293.
    • (1978) FEBS Lett , vol.92 , pp. 287-293
    • Cohen, P.1    Burchell, A.2    Foulkes, J.G.3    Cohen, P.T.4
  • 11
    • 0024341971 scopus 로고
    • The g-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin
    • Dasgupta, M., Honeycutt, T., and Blumenthal, D.K. 1989. The g-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin. J. Biol. Chem. 264: 17156-17163.
    • (1989) J. Biol. Chem , vol.264 , pp. 17156-17163
    • Dasgupta, M.1    Honeycutt, T.2    Blumenthal, D.K.3
  • 12
    • 0018662301 scopus 로고
    • Calcium and calmodulin activation of muscle phosphorylase kinase: Effect of tryptic proteolysis
    • Depaoli-Roach, A.A., Gibbs, J.B., and Roach, P.J. 1979a. Calcium and calmodulin activation of muscle phosphorylase kinase: Effect of tryptic proteolysis. FEBS Lett. 105: 321-324.
    • (1979) FEBS Lett , vol.105 , pp. 321-324
    • Depaoli-Roach, A.A.1    Gibbs, J.B.2    Roach, P.J.3
  • 13
    • 0018391685 scopus 로고
    • Rabbit skeletal muscle phosphorylase kinase. Comparison of glycogen synthase and phosphorylase as substrates
    • DePaoli-Roach, A.A., Roach, P.J., and Larner, J. 1979b. Rabbit skeletal muscle phosphorylase kinase. Comparison of glycogen synthase and phosphorylase as substrates. J. Biol. Chem. 254: 4212-4219.
    • (1979) J. Biol. Chem , vol.254 , pp. 4212-4219
    • DePaoli-Roach, A.A.1    Roach, P.J.2    Larner, J.3
  • 14
    • 0141594755 scopus 로고    scopus 로고
    • A closed compact structure of native Ca(2+)-calmodulin
    • Fallon, J.L. and Quiocho, F.A. 2003. A closed compact structure of native Ca(2+)-calmodulin. Structure 11: 1303-1307.
    • (2003) Structure , vol.11 , pp. 1303-1307
    • Fallon, J.L.1    Quiocho, F.A.2
  • 17
    • 33845261364 scopus 로고    scopus 로고
    • Calmodulin, conformational states, and calcium signaling. A single-molecule perspective
    • Johnson, C.K. 2006. Calmodulin, conformational states, and calcium signaling. A single-molecule perspective. Biochemistry 45: 14233-14246.
    • (2006) Biochemistry , vol.45 , pp. 14233-14246
    • Johnson, C.K.1
  • 18
    • 0019877640 scopus 로고
    • Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions
    • King, M.M. and Carlson, G.M. 1981. Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions. J. Biol. Chem. 256: 11058-11064.
    • (1981) J. Biol. Chem , vol.256 , pp. 11058-11064
    • King, M.M.1    Carlson, G.M.2
  • 20
    • 0030704677 scopus 로고    scopus 로고
    • Differential affinity crosslinking of phosphorylase kinase conformers by the geometric isomers of phenylenedimaleimide
    • Nadeau, O.W., Sacks, D.B., and Carlson, G.M. 1997. Differential affinity crosslinking of phosphorylase kinase conformers by the geometric isomers of phenylenedimaleimide. J. Biol. Chem. 272: 26196-26201.
    • (1997) J. Biol. Chem , vol.272 , pp. 26196-26201
    • Nadeau, O.W.1    Sacks, D.B.2    Carlson, G.M.3
  • 21
    • 0033596745 scopus 로고    scopus 로고
    • Activators of phosphorylase kinase alter the cross-linking of its catalytic subunit to the C-terminal one-sixth of its regulatory a subunit
    • Nadeau, O.W., Traxler, K.W., Fee, L.R., Baldwin, B.A., and Carlson, G.M. 1999. Activators of phosphorylase kinase alter the cross-linking of its catalytic subunit to the C-terminal one-sixth of its regulatory a subunit. Biochemistry 38: 2551-2559.
    • (1999) Biochemistry , vol.38 , pp. 2551-2559
    • Nadeau, O.W.1    Traxler, K.W.2    Fee, L.R.3    Baldwin, B.A.4    Carlson, G.M.5
  • 22
    • 0036153608 scopus 로고    scopus 로고
    • A Ca(2+)-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy
    • Nadeau, O.W., Carlson, G.M., and Gogol, E.P. 2002. A Ca(2+)-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy. Structure 10: 23-32.
    • (2002) Structure , vol.10 , pp. 23-32
    • Nadeau, O.W.1    Carlson, G.M.2    Gogol, E.P.3
  • 23
    • 15244350753 scopus 로고    scopus 로고
    • Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase
    • Nadeau, O.W., Gogol, E.P., and Carlson, G.M. 2005. Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase. Protein Sci. 14: 914-920.
    • (2005) Protein Sci , vol.14 , pp. 914-920
    • Nadeau, O.W.1    Gogol, E.P.2    Carlson, G.M.3
  • 24
    • 0028133157 scopus 로고
    • Structure of phosphorylase kinase. A three-dimensional model derived from stained and unstained electron micrographs
    • Norcum, M.T., Wilkinson, D.A., Carlson, M.C., Hainfeld, J.F., and Carlson, G.M. 1994. Structure of phosphorylase kinase. A three-dimensional model derived from stained and unstained electron micrographs. J. Mol. Biol. 241: 94-102.
    • (1994) J. Mol. Biol , vol.241 , pp. 94-102
    • Norcum, M.T.1    Wilkinson, D.A.2    Carlson, M.C.3    Hainfeld, J.F.4    Carlson, G.M.5
  • 25
    • 0019137715 scopus 로고
    • Phosphorylase kinase from rabbit skeletal muscle: Identification of the calmodulin-binding subunits
    • Picton, C., Klee, C.B., and Cohen, P. 1980. Phosphorylase kinase from rabbit skeletal muscle: Identification of the calmodulin-binding subunits. Eur. J. Biochem. 111: 553-561.
    • (1980) Eur. J. Biochem , vol.111 , pp. 553-561
    • Picton, C.1    Klee, C.B.2    Cohen, P.3
  • 26
    • 15244341312 scopus 로고    scopus 로고
    • Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering
    • Priddy, T.S., MacDonald, B.A., Heller, W.T., Nadeau, O.W., Trewhella, J., and Carlson, G.M. 2005. Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering. Protein Sci. 14: 1039-1048.
    • (2005) Protein Sci , vol.14 , pp. 1039-1048
    • Priddy, T.S.1    MacDonald, B.A.2    Heller, W.T.3    Nadeau, O.W.4    Trewhella, J.5    Carlson, G.M.6
  • 27
    • 0018600127 scopus 로고
    • The role of calmodulin in the structure and regulation of phosphorylase kinase from rabbit skeletal muscle
    • Shenolikar, S., Cohen, P.T., Cohen, P., Nairn, A.C., and Perry, S.V. 1979. The role of calmodulin in the structure and regulation of phosphorylase kinase from rabbit skeletal muscle. Eur. J. Biochem. 100: 329-337.
    • (1979) Eur. J. Biochem , vol.100 , pp. 329-337
    • Shenolikar, S.1    Cohen, P.T.2    Cohen, P.3    Nairn, A.C.4    Perry, S.V.5
  • 28
    • 3442896792 scopus 로고    scopus 로고
    • Single-molecule resonance energy transfer and fluorescence correlation spectroscopy of calmodulin in solution
    • Slaughter, B.D., Allen, M.W., Unruh, J.R., Bieber-Urbauer, R.J., and Johnson, C.K. 2004. Single-molecule resonance energy transfer and fluorescence correlation spectroscopy of calmodulin in solution. J. Phys. Chem. B 108: 10388-10397.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 10388-10397
    • Slaughter, B.D.1    Allen, M.W.2    Unruh, J.R.3    Bieber-Urbauer, R.J.4    Johnson, C.K.5
  • 29
    • 22344451979 scopus 로고    scopus 로고
    • Singlemolecule tracking of sub-millisecond domain motion in calmodulin
    • Slaughter, B.D., Bieber-Urbauer, R.J., and Johnson, C.K. 2005a. Singlemolecule tracking of sub-millisecond domain motion in calmodulin. J. Phys. Chem. B 109: 12658-12662.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 12658-12662
    • Slaughter, B.D.1    Bieber-Urbauer, R.J.2    Johnson, C.K.3
  • 30
    • 14844352643 scopus 로고    scopus 로고
    • Conformational substates of calmodulin revealed by single-pair fluorescence resonance energy transfer: Influence of solution conditions and oxidative modification
    • Slaughter, B.D., Unruh, J.R., Allen, M.W., Bieber Urbauer, R.J., and Johnson, C.K. 2005b. Conformational substates of calmodulin revealed by single-pair fluorescence resonance energy transfer: Influence of solution conditions and oxidative modification. Biochemistry 44: 3694-3707.
    • (2005) Biochemistry , vol.44 , pp. 3694-3707
    • Slaughter, B.D.1    Unruh, J.R.2    Allen, M.W.3    Bieber Urbauer, R.J.4    Johnson, C.K.5
  • 31
    • 0035783345 scopus 로고    scopus 로고
    • Direct visualization of the calmodulin subunit of phosphorylase kinase via electron microscopy following subunit exchange
    • Traxler, K.W., Norcum, M.T., Hainfeld, J.F., and Carlson, G.M. 2001. Direct visualization of the calmodulin subunit of phosphorylase kinase via electron microscopy following subunit exchange. J. Struct. Biol. 135: 231-238.
    • (2001) J. Struct. Biol , vol.135 , pp. 231-238
    • Traxler, K.W.1    Norcum, M.T.2    Hainfeld, J.F.3    Carlson, G.M.4
  • 32
    • 0025088855 scopus 로고
    • Smallangle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase
    • Trewhella, J., Blumenthal, D.K., Rokop, S.E., and Seeger, P.A. 1990. Smallangle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase. Biochemistry 29: 9316-9324.
    • (1990) Biochemistry , vol.29 , pp. 9316-9324
    • Trewhella, J.1    Blumenthal, D.K.2    Rokop, S.E.3    Seeger, P.A.4
  • 33
    • 0036155785 scopus 로고    scopus 로고
    • Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b
    • Venien-Bryan, C., Lowe, E.M., Boisset, N., Traxler, K.W., Johnson, L.N., and Carlson, G.M. 2002. Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b. Structure 10: 33-41.
    • (2002) Structure , vol.10 , pp. 33-41
    • Venien-Bryan, C.1    Lowe, E.M.2    Boisset, N.3    Traxler, K.W.4    Johnson, L.N.5    Carlson, G.M.6
  • 34
    • 0024445873 scopus 로고
    • Computational and sitespecific mutagenesis analyses of the asymmetric charge distribution on calmodulin
    • Weber, P.C., Lukas, T.J., Craig, T.A., Wilson, E., King, M.M., Kwiatkowski, A.P., and Watterson, D.M. 1989. Computational and sitespecific mutagenesis analyses of the asymmetric charge distribution on calmodulin. Proteins 6: 70-85.
    • (1989) Proteins , vol.6 , pp. 70-85
    • Weber, P.C.1    Lukas, T.J.2    Craig, T.A.3    Wilson, E.4    King, M.M.5    Kwiatkowski, A.P.6    Watterson, D.M.7
  • 35
    • 0028180371 scopus 로고
    • An epitope proximal to the carboxyl terminus of the a-subunit is located near the lobe tips of the phosphorylase kinase hexadecamer
    • Wilkinson, D.A., Marion, T.N., Tillman, D.M., Norcum, M.T., Hainfeld, J.F., Seyer, J.M., and Carlson, G.M. 1994. An epitope proximal to the carboxyl terminus of the a-subunit is located near the lobe tips of the phosphorylase kinase hexadecamer. J. Mol. Biol. 235: 974-982.
    • (1994) J. Mol. Biol , vol.235 , pp. 974-982
    • Wilkinson, D.A.1    Marion, T.N.2    Tillman, D.M.3    Norcum, M.T.4    Hainfeld, J.F.5    Seyer, J.M.6    Carlson, G.M.7
  • 36
    • 0031046054 scopus 로고    scopus 로고
    • Proximal regions of the catalytic g and regulatory b subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation
    • Wilkinson, D.A., Norcum, M.T., Fizgerald, T.J., Marion, T.N., Tillman, D.M., and Carlson, G.M. 1997. Proximal regions of the catalytic g and regulatory b subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation. J. Mol. Biol. 265: 319-329.
    • (1997) J. Mol. Biol , vol.265 , pp. 319-329
    • Wilkinson, D.A.1    Norcum, M.T.2    Fizgerald, T.J.3    Marion, T.N.4    Tillman, D.M.5    Carlson, G.M.6
  • 37
    • 0028232698 scopus 로고
    • Resolution of structural changes associated with calcium activation of calmodulin using frequency domain fluorescence spectroscopy
    • Yao, Y., Schoneich, C., and Squier, T.C. 1994. Resolution of structural changes associated with calcium activation of calmodulin using frequency domain fluorescence spectroscopy. Biochemistry 33: 7797-7810.
    • (1994) Biochemistry , vol.33 , pp. 7797-7810
    • Yao, Y.1    Schoneich, C.2    Squier, T.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.