메뉴 건너뛰기




Volumn 1830, Issue 4, 2013, Pages 2899-2906

Insights into eukaryotic Rubisco assembly - Crystal structures of RbcX chaperones from Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; RbcX; Rubisco assembly

Indexed keywords

CHAPERONE; PROTEIN RBCX1; PROTEIN RBCX2; RIBULOSEBISPHOSPHATE CARBOXYLASE; UNCLASSIFIED DRUG;

EID: 84873738356     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.12.025     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 79551571754 scopus 로고    scopus 로고
    • Oxygenic photosynthesis and the distribution of chloroplasts
    • E. Gantt Oxygenic photosynthesis and the distribution of chloroplasts Photosynth. Res. 107 2011 1 6
    • (2011) Photosynth. Res. , vol.107 , pp. 1-6
    • Gantt, E.1
  • 2
    • 0037001963 scopus 로고    scopus 로고
    • Complex evolution of photosynthesis
    • J. Xiong, and C.E. Bauer Complex evolution of photosynthesis Annu. Rev. Plant Biol. 53 2002 503 521
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 503-521
    • Xiong, J.1    Bauer, C.E.2
  • 3
    • 44649180586 scopus 로고    scopus 로고
    • Catalysis and regulation in Rubisco
    • I. Andersson Catalysis and regulation in Rubisco J. Exp. Bot. 59 2008 1555 1568
    • (2008) J. Exp. Bot. , vol.59 , pp. 1555-1568
    • Andersson, I.1
  • 6
    • 34250017377 scopus 로고    scopus 로고
    • Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco
    • S. Saschenbrecker, A. Bracher, K.V. Rao, B.V. Rao, F.U. Hartl, and M. Hayer-Hartl Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco Cell 129 2007 1189 1200
    • (2007) Cell , vol.129 , pp. 1189-1200
    • Saschenbrecker, S.1    Bracher, A.2    Rao, K.V.3    Rao, B.V.4    Hartl, F.U.5    Hayer-Hartl, M.6
  • 9
    • 79953715968 scopus 로고    scopus 로고
    • Mechanism of plastid division: From a bacterium to an organelle
    • S.Y. Miyagishima Mechanism of plastid division: from a bacterium to an organelle Plant Physiol. 155 2011 1533 1544
    • (2011) Plant Physiol. , vol.155 , pp. 1533-1544
    • Miyagishima, S.Y.1
  • 10
    • 79955597646 scopus 로고    scopus 로고
    • Divergent evolutionary fates of major photosynthetic gene networks following gene and whole genome duplications
    • J.E. Coate, and J.J. Doyle Divergent evolutionary fates of major photosynthetic gene networks following gene and whole genome duplications Plant Signal. Behav. 6 2011 594 597
    • (2011) Plant Signal. Behav. , vol.6 , pp. 594-597
    • Coate, J.E.1    Doyle, J.J.2
  • 11
    • 80054020146 scopus 로고    scopus 로고
    • Initial characteristics of RbcX proteins from Arabidopsis thaliana
    • P. Kolesinski, J. Piechota, and A. Szczepaniak Initial characteristics of RbcX proteins from Arabidopsis thaliana Plant Mol. Biol. 77 2011 447 459
    • (2011) Plant Mol. Biol. , vol.77 , pp. 447-459
    • Kolesinski, P.1    Piechota, J.2    Szczepaniak, A.3
  • 12
    • 33845492890 scopus 로고    scopus 로고
    • The open-access high-throughput crystallization facility at EMBL Hamburg
    • J. Mueller-Dieckmann The open-access high-throughput crystallization facility at EMBL Hamburg Acta Crystallogr. D Biol. Crystallogr. 62 2006 1446 1452
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1446-1452
    • Mueller-Dieckmann, J.1
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 20
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • I.N. Shindyalov, and P.E. Bourne Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng. 11 1998 739 747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 21
    • 4444351490 scopus 로고    scopus 로고
    • Empirical force fields for biological macromolecules: Overview and issues
    • A.D. Mackerell Empirical force fields for biological macromolecules: overview and issues J. Comput. Chem. 25 2004 1584 1604
    • (2004) J. Comput. Chem. , vol.25 , pp. 1584-1604
    • Mackerell, A.D.1
  • 26
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals - A new molecular-dynamics method
    • M. Parrinello, and A. Rahman Polymorphic transitions in single-crystals - a new molecular-dynamics method J. Appl. Phys. 52 1981 7182 7190
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 27
    • 0001538909 scopus 로고
    • Canonical dynamics - Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics - equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 28
    • 84943502952 scopus 로고
    • A molecular-dynamics method for simulations in the canonical ensemble
    • S. Nose A molecular-dynamics method for simulations in the canonical ensemble Mol. Phys. 52 1984 255 268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nose, S.1
  • 29
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 30
    • 51149113756 scopus 로고    scopus 로고
    • Rational 'correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization
    • M. Tarnawski, S. Krzywda, A. Szczepaniak, and M. Jaskolski Rational 'correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization Acta Crystallogr. F Struct. Biol. Cryst. Commun. 64 2008 870 874
    • (2008) Acta Crystallogr. F Struct. Biol. Cryst. Commun. , vol.64 , pp. 870-874
    • Tarnawski, M.1    Krzywda, S.2    Szczepaniak, A.3    Jaskolski, M.4
  • 31
    • 0037267882 scopus 로고    scopus 로고
    • Chloroplast redox signals: How photosynthesis controls its own genes
    • T. Pfannschmidt Chloroplast redox signals: how photosynthesis controls its own genes Trends Plant Sci. 8 1 2003 33 41
    • (2003) Trends Plant Sci. , vol.8 , Issue.1 , pp. 33-41
    • Pfannschmidt, T.1
  • 33
    • 0033133350 scopus 로고    scopus 로고
    • BUNDLE SHEATH DEFECTIVE2, a novel protein required for post-translational regulation of the rbcL gene of maize
    • T.P. Brutnell, R.J. Sawers, A. Mant, and J.A. Langdale BUNDLE SHEATH DEFECTIVE2, a novel protein required for post-translational regulation of the rbcL gene of maize Plant Cell 11 5 1999 849 864
    • (1999) Plant Cell , vol.11 , Issue.5 , pp. 849-864
    • Brutnell, T.P.1    Sawers, R.J.2    Mant, A.3    Langdale, J.A.4
  • 34
    • 84867032700 scopus 로고    scopus 로고
    • Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize
    • L. Feiz, R. Williams-Carrier, K. Wostrikoff, S. Belcher, A. Barkan, and D.B. Stern Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize Plant Cell 24 8 2012 3435 3446
    • (2012) Plant Cell , vol.24 , Issue.8 , pp. 3435-3446
    • Feiz, L.1    Williams-Carrier, R.2    Wostrikoff, K.3    Belcher, S.4    Barkan, A.5    Stern, D.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.