메뉴 건너뛰기




Volumn 91, Issue 3, 2009, Pages 401-407

Hierarchy in guanidine unfolding of DLC8 dimer: Regulatory functional implications

Author keywords

Circular dichroism; Dynein light chain protein; Fluorescence spectroscopy; Monomeric intermediate; Nuclear magnetic resonance; Protein folding

Indexed keywords

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; DYNEIN ATPASE; GUANIDINE; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE;

EID: 60249083739     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.10.013     Document Type: Article
Times cited : (9)

References (23)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 9944220618 scopus 로고    scopus 로고
    • Rewiring cell signaling: the logic and plasticity of eukaryotic protein circuitry
    • Dueber J.E., Yeh B.J., Bhattacharyya R.P., and Lim W.A. Rewiring cell signaling: the logic and plasticity of eukaryotic protein circuitry. Curr. Opin. Struct. Biol. 14 (2004) 690-699
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 690-699
    • Dueber, J.E.1    Yeh, B.J.2    Bhattacharyya, R.P.3    Lim, W.A.4
  • 3
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 4
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., and Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4 (1997) 10-19
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 5
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: an ancient motor protein involved in multiple modes of transport
    • Vallee R.B., Williams J.C., Varma D., and Barnhart L.E. Dynein: an ancient motor protein involved in multiple modes of transport. J. Neurobiol. 58 (2004) 189-200
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 6
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif
    • Lo K.W., Naisbitt S., Fan J.S., Sheng M., and Zhang M. The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif. J. Biol. Chem. 276 (2001) 14059-14066
    • (2001) J. Biol. Chem. , vol.276 , pp. 14059-14066
    • Lo, K.W.1    Naisbitt, S.2    Fan, J.S.3    Sheng, M.4    Zhang, M.5
  • 8
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G., Coultas L., Cheney R.E., Huang D.C., and Strasser A. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 293 (2001) 1829-1832
    • (2001) Science , vol.293 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.7    Strasser, A.8
  • 10
    • 31344449610 scopus 로고    scopus 로고
    • pH driven conformational dynamics and dimer-to-monomer transition in DLC8
    • Mohan P.M., Barve M., Chatterjee A., and Hosur R.V. pH driven conformational dynamics and dimer-to-monomer transition in DLC8. Protein Sci. 15 (2006) 335-342
    • (2006) Protein Sci. , vol.15 , pp. 335-342
    • Mohan, P.M.1    Barve, M.2    Chatterjee, A.3    Hosur, R.V.4
  • 11
    • 0142039800 scopus 로고    scopus 로고
    • Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly
    • Wang W., Lo K.W., Kan H.M., Fan J.S., and Zhang M. Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly. J. Biol. Chem. 278 (2003) 41491-41499
    • (2003) J. Biol. Chem. , vol.278 , pp. 41491-41499
    • Wang, W.1    Lo, K.W.2    Kan, H.M.3    Fan, J.S.4    Zhang, M.5
  • 12
    • 33847660005 scopus 로고    scopus 로고
    • NMR insights into dynamics regulated target binding of DLC8 dimer
    • Krishna Mohan P.M., and Hosur R.V. NMR insights into dynamics regulated target binding of DLC8 dimer. Biochem. Biophys. Res. Commun. 355 (2007) 950-955
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 950-955
    • Krishna Mohan, P.M.1    Hosur, R.V.2
  • 13
    • 27444442808 scopus 로고    scopus 로고
    • Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation
    • Nyarko A., Cochrun L., Norwood S., Pursifull N., Voth A., and Barbar E. Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation. Biochemistry 44 (2005) 14248-14255
    • (2005) Biochemistry , vol.44 , pp. 14248-14255
    • Nyarko, A.1    Cochrun, L.2    Norwood, S.3    Pursifull, N.4    Voth, A.5    Barbar, E.6
  • 14
    • 34447127515 scopus 로고    scopus 로고
    • Potential role for phosphorylation in differential regulation of the assembly of dynein light chains
    • Song Y., Benison G., Nyarko A., Hays T.S., and Barbar E. Potential role for phosphorylation in differential regulation of the assembly of dynein light chains. J. Biol. Chem. 282 (2007) 17272-17279
    • (2007) J. Biol. Chem. , vol.282 , pp. 17272-17279
    • Song, Y.1    Benison, G.2    Nyarko, A.3    Hays, T.S.4    Barbar, E.5
  • 15
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar E., Kleinman B., Imhoff D., Li M., Hays T.S., and Hare M. Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry 40 (2001) 1596-1605
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.S.5    Hare, M.6
  • 16
    • 33845679781 scopus 로고    scopus 로고
    • Equilibrium unfolding of DLC8 monomer by urea and guanidine hydrochloride: distinctive global and residue level features
    • Chatterjee A., Krishna Mohan P.M., Prabhu A., Ghosh-Roy A., and Hosur R.V. Equilibrium unfolding of DLC8 monomer by urea and guanidine hydrochloride: distinctive global and residue level features. Biochimie 89 (2007) 117-134
    • (2007) Biochimie , vol.89 , pp. 117-134
    • Chatterjee, A.1    Krishna Mohan, P.M.2    Prabhu, A.3    Ghosh-Roy, A.4    Hosur, R.V.5
  • 17
    • 35248900503 scopus 로고    scopus 로고
    • Unfolding energetics and conformational stability of DLC8 monomer
    • Krishna Mohan P.M. Unfolding energetics and conformational stability of DLC8 monomer. Biochimie 89 (2007) 1409-1415
    • (2007) Biochimie , vol.89 , pp. 1409-1415
    • Krishna Mohan, P.M.1
  • 19
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 20
    • 0030711517 scopus 로고    scopus 로고
    • Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
    • Grimsley J.K., Scholtz J.M., Pace C.N., and Wild J.R. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. Biochemistry 36 (1997) 14366-14374
    • (1997) Biochemistry , vol.36 , pp. 14366-14374
    • Grimsley, J.K.1    Scholtz, J.M.2    Pace, C.N.3    Wild, J.R.4
  • 23
    • 44949253210 scopus 로고    scopus 로고
    • NMR characterization of structural and dynamics perturbations due to a single point mutation in Drosophila DLC8 dimer: functional implications
    • Mohan P.M., and Hosur R.V. NMR characterization of structural and dynamics perturbations due to a single point mutation in Drosophila DLC8 dimer: functional implications. Biochemistry 47 (2008) 6251-6259
    • (2008) Biochemistry , vol.47 , pp. 6251-6259
    • Mohan, P.M.1    Hosur, R.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.