메뉴 건너뛰기




Volumn 4, Issue MAY, 2015, Pages

A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress related acidosis

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; HOLDASE; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG; ALPHA CRYSTALLIN; CHAPERONE; CRYAB PROTEIN, HUMAN;

EID: 84930629588     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.07304     Document Type: Article
Times cited : (49)

References (38)
  • 2
    • 0141703310 scopus 로고    scopus 로고
    • Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers alphaB-crystallin
    • AQUILINA, J. A., BENESCH, J. L., BATEMAN, O. A., SLINGSBY, C. & ROBINSON, C. V. 2003. Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers alphaB-crystallin. Proc Natl Acad Sci U S A, 100, 10611-6.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 3
    • 80054722790 scopus 로고    scopus 로고
    • Quaternary dynamics of alphaB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus
    • BALDWIN, A. J., HILTON, G. R., LIOE, H., BAGNERIS, C., BENESCH, J. L. & KAY, L. E. 2011a. Quaternary dynamics of alphaB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. J Mol Biol, 413, 310-20.
    • (2011) J Mol Biol , vol.413 , pp. 310-320
    • Baldwin, A.J.1    Hilton, G.R.2    Lioe, H.3    Bagneris, C.4    Benesch, J.L.5    Kay, L.E.6
  • 4
    • 80054746164 scopus 로고    scopus 로고
    • alphaB crystallin polydispersity is a consequence of unbiased quaternary dynamics
    • BALDWIN, A. J., LIOE, H., ROBINSON, C. V., KAY, L. E. & BENESCH, J. L. 2011b. alphaB crystallin polydispersity is a consequence of unbiased quaternary dynamics. J Mol Biol, 413, 297- 309.
    • (2011) J Mol Biol , vol.413 , pp. 297-309
    • Baldwin, A.J.1    Lioe, H.2    Robinson, C.V.3    Kay, L.E.4    Benesch, J.L.5
  • 5
    • 79960698253 scopus 로고    scopus 로고
    • Three-dimensional structure of alpha-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6
    • BARANOVA, E. V., WEEKS, S. D., BEELEN, S., BUKACH, O. V., GUSEV,, N. B. & STRELKOV, S. V. 2011. Three-dimensional structure of alpha-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6. J Mol Biol, 411, 110-22.
    • (2011) J Mol Biol , vol.411 , pp. 110-122
    • Baranova, E.V.1    Weeks, S.D.2    Beelen, S.3    Bukach, O.V.4    Gusev, N.B.5    Strelkov, S.V.6
  • 6
    • 0022322979 scopus 로고
    • Direct measurement of pH in the rat lens by ion-sensitive microelectrodes
    • BASSNETT, S. & DUNCAN, G. 1985. Direct measurement of pH in the rat lens by ion-sensitive microelectrodes. Exp Eye Res, 40, 585-90.
    • (1985) Exp Eye Res , vol.40 , pp. 585-590
    • Bassnett, S.1    Duncan, G.2
  • 8
    • 79953253901 scopus 로고    scopus 로고
    • Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove
    • CLARK, A. R., NAYLOR, C. E., BAGNERIS, C., KEEP, N. H. & SLINGSBY, C. 2011. Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove. J Mol Biol, 408, 118-34.
    • (2011) J Mol Biol , vol.408 , pp. 118-134
    • Clark, A.R.1    Naylor, C.E.2    Bagneris, C.3    Keep, N.H.4    Slingsby, C.5
  • 9
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • DELAGLIO, F., GRZESIEK, S., VUISTER, G. W., ZHU, G., PFEIFER, J. & BAX, A. 1995. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR, 6, 277-93.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 10
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • FRANK, J., RADERMACHER, M., PENCZEK, P., ZHU, J., LI, Y., LADJADJ, M. & LEITH, A. 1996. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol, 116, 190-9.
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 11
    • 21744436278 scopus 로고    scopus 로고
    • The activation mechanism of Hsp26 does not require dissociation of the oligomer
    • FRANZMANN, T. M., WUHR, M., RICHTER, K., WALTER, S. & BUCHNER, J. 2005. The activation mechanism of Hsp26 does not require dissociation of the oligomer. J Mol Biol, 350, 1083-93.
    • (2005) J Mol Biol , vol.350 , pp. 1083-1093
    • Franzmann, T.M.1    Wuhr, M.2    Richter, K.3    Walter, S.4    Buchner, J.5
  • 12
    • 84904393444 scopus 로고    scopus 로고
    • Dynamical structure of alphaB-crystallin
    • HOCHBERG, G. K. & BENESCH, J. L. 2014. Dynamical structure of alphaB-crystallin. Prog Biophys Mol Biol, 115, 11-20.
    • (2014) Prog Biophys Mol Biol , vol.115 , pp. 11-20
    • Hochberg, G.K.1    Benesch, J.L.2
  • 14
    • 58549087803 scopus 로고    scopus 로고
    • alphaB-crystallin: A hybrid solid state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer
    • JEHLE, S., VAN ROSSUM, B., STOUT, J. R., NOGUCHI, S. M., FALBER, K., REHBEIN, K., OSCHKINAT, H., KLEVIT, R. E. & RAJAGOPAL, P. 2009. alphaB-crystallin: a hybrid solid state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer. J Mol Biol, 385, 1481-97.
    • (2009) J Mol Biol , vol.385 , pp. 1481-1497
    • Jehle, S.1    Van Rossum, B.2    Stout, J.R.3    Noguchi, S.M.4    Falber, K.5    Rehbein, K.6    Oschkinat, H.7    Klevit, R.E.8    Rajagopal, P.9
  • 16
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • JOHNSON, B. A. 2004. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol, 278, 313-52.
    • (2004) Methods Mol Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 17
    • 84864456309 scopus 로고    scopus 로고
    • HSPBs: Small proteins with big implications in human disease
    • KAMPINGA, H. H. & GARRIDO, C. 2012. HSPBs: small proteins with big implications in human disease. Int J Biochem Cell Biol, 44, 1706-10.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1706-1710
    • Kampinga, H.H.1    Garrido, C.2
  • 18
    • 79958837339 scopus 로고    scopus 로고
    • An introduction to NMR-based approaches for measuring protein dynamics
    • KLECKNER, I. R. & FOSTER, M. P. 2011. An introduction to NMR-based approaches for measuring protein dynamics. Biochim Biophys Acta, 1814, 942-68.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 942-968
    • Kleckner, I.R.1    Foster, M.P.2
  • 19
    • 84856520247 scopus 로고    scopus 로고
    • GUARDD: User-friendly MATLAB software for rigorous analysis of CPMG RD NMR data
    • KLECKNER, I. R. & FOSTER, M. P. 2012. GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data. J Biomol NMR, 52, 11-22.
    • (2012) J Biomol NMR , vol.52 , pp. 11-22
    • Kleckner, I.R.1    Foster, M.P.2
  • 21
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • LEE, G. J., ROSEMAN, A. M., SAIBIL, H. R. & VIERLING, E. 1997. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J, 16, 659-71.
    • (1997) EMBO J , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 22
    • 84855478926 scopus 로고    scopus 로고
    • Structural and mechanistic implications of metal binding in the small heat-shock protein alphaB-crystallin
    • MAINZ, A., BARDIAUX, B., KUPPLER, F., MULTHAUP, G., FELLI, I. C., PIERATTELLI, R. & REIF, B. 2012. Structural and mechanistic implications of metal binding in the small heat-shock protein alphaB-crystallin. J Biol Chem, 287, 1128-38.
    • (2012) J Biol Chem , vol.287 , pp. 1128-1138
    • Mainz, A.1    Bardiaux, B.2    Kuppler, F.3    Multhaup, G.4    Felli, I.C.5    Pierattelli, R.6    Reif, B.7
  • 23
    • 0026348012 scopus 로고
    • Cell to cell communication mmunication and pH in the frog lens
    • MATHIAS, R. T., RIQUELME, G. & RAE, J. L. 1991. Cell to cell communication mmunication and pH in the frog lens. J Gen Physiol, 98, 1085-103.
    • (1991) J Gen Physiol , vol.98 , pp. 1085-1103
    • Mathias, R.T.1    Riquelme, G.2    Rae, J.L.3
  • 25
    • 84897574971 scopus 로고    scopus 로고
    • Quantitative tissue pH measurement during cerebral ischemia using amine and amide concentration-independent detection (AACID) with MRI
    • MCVICAR, N., LI, A. X., GONCALVES, D. F., BELLYOU, M., MEAKIN, S. O., PRADO, M. A. & BARTHA, R. 2014. Quantitative tissue pH measurement during cerebral ischemia using amine and amide concentration-independent detection (AACID) with MRI. J Cereb Blood Flow Metab, 34, 690-8.
    • (2014) J Cereb Blood Flow Metab , vol.34 , pp. 690-698
    • McVicar, N.1    Li, A.X.2    Goncalves, D.F.3    Bellyou, M.4    Meakin, S.O.5    Prado, M.A.6    Bartha, R.7
  • 26
    • 84879689977 scopus 로고    scopus 로고
    • Physico-chemical properties of R140G and K141Q mutants of human small heat shock protein HspB1 associated with hereditary peripheral neuropathies
    • NEFEDOVA, V. V., DATSKEVICH, P. N., SUDNITSYNA, M. V., STRELKOV, S. V. & GUSEV, N. B. 2013. Physico-chemical properties of R140G and K141Q mutants of human small heat shock protein HspB1 associated with hereditary peripheral neuropathies. Biochimie, 95, 1582-92.
    • (2013) Biochimie , vol.95 , pp. 1582-1592
    • Nefedova, V.V.1    Datskevich, P.N.2    Sudnitsyna, M.V.3    Strelkov, S.V.4    Gusev, N.B.5
  • 27
    • 0026607545 scopus 로고
    • Kinetics of protein-protein association explained by Brownian dynamics computer simulation
    • NORTHRUP, S. H. & ERICKSON, H. P. 1992. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc Natl Acad Sci U S A, 89, 3338-42.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 3338-3342
    • Northrup, S.H.1    Erickson, H.P.2
  • 28
    • 2342662152 scopus 로고    scopus 로고
    • Negative Staining and Image Classification - Powerful Tools in Modern Electron Microscopy
    • OHI, M., LI, Y., CHENG, Y. & WALZ, T. 2004. Negative Staining and Image Classification - Powerful Tools in Modern Electron Microscopy. Biol Proced Online, 6, 23-34.
    • (2004) Biol Proced Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 29
    • 0027456412 scopus 로고
    • Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • PELTON, J. G., TORCHIA, D. A., MEADOW, N. D. & ROSEMAN, S. 1993. Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci, 2, 543-58.
    • (1993) Protein Sci , vol.2 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 32
    • 21644459373 scopus 로고    scopus 로고
    • Progress in protein-protein docking: Atomic resolution predictions in the CAPRI experiment using RosettaDock with an improved treatment of side-chain flexibility
    • SCHUELER-FURMAN, O., WANG, C. & BAKER, D. 2005. Progress in protein-protein docking: atomic resolution predictions in the CAPRI experiment using RosettaDock with an improved treatment of side-chain flexibility. Proteins, 60, 187-94.
    • (2005) Proteins , vol.60 , pp. 187-194
    • Schueler-Furman, O.1    Wang, C.2    Baker, D.3
  • 33
    • 79954990720 scopus 로고    scopus 로고
    • Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings
    • SGOURAKIS, N. G., LANGE, O. F., DIMAIO, F., ANDRE, I., FITZKEE, N. C., ROSSI, P., MONTELIONE, G. T., BAX, A. & BAKER, D. 2011. Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings. J Am Chem Soc, 133, 6288-98.
    • (2011) J Am Chem Soc , vol.133 , pp. 6288-6298
    • Sgourakis, N.G.1    Lange, O.F.2    Dimaio, F.3    Andre, I.4    Fitzkee, N.C.5    Rossi, P.6    Montelione, G.T.7    Bax, A.8    Baker, D.9
  • 36
    • 84892938306 scopus 로고    scopus 로고
    • Improved chemical shift based fragment selection for CS-Rosetta using Rosetta3 fragment picker
    • VERNON, R., SHEN, Y., BAKER, D. & LANGE, O. F. 2013. Improved chemical shift based fragment selection for CS-Rosetta using Rosetta3 fragment picker. J Biomol NMR, 57, 117-27.
    • (2013) J Biomol NMR , vol.57 , pp. 117-127
    • Vernon, R.1    Shen, Y.2    Baker, D.3    Lange, O.F.4
  • 38
    • 2942653357 scopus 로고    scopus 로고
    • Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases
    • ZWECKSTETTER, M., HUMMER, G. & BAX, A. 2004. Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases. Biophys J, 86, 3444-60.
    • (2004) Biophys J , vol.86 , pp. 3444-3460
    • Zweckstetter, M.1    Hummer, G.2    Bax, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.