메뉴 건너뛰기




Volumn 115, Issue 2, 1996, Pages 191-197

Cycloheximide retards high light driven D1 protein degradation in Chlamydomonas reinhardtii

Author keywords

Chlamydomonas reinhardtii; D1 protein; Photoinhibition; Photosystem II; Protein degradation

Indexed keywords


EID: 0013492499     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/0168-9452(96)04345-2     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 0000226607 scopus 로고
    • Dynamics of photosystem II: Mechanism of photoinhibition and recovery processes (1992)
    • J. Barber (Ed.), Elsevier, Amsterdam
    • O. Prásil, N. Adir and I. Ohad, Dynamics of photosystem II: mechanism of photoinhibition and recovery processes (1992) in: J. Barber (Ed.), The Photosystems: Structure. Function and Molecular Biology, Vol. 11, Elsevier, Amsterdam, 1992, pp. 295-348.
    • (1992) The Photosystems: Structure. Function and Molecular Biology , vol.11 , pp. 295-348
    • Prásil, O.1    Adir, N.2    Ohad, I.3
  • 2
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • E.-M. Aro, I. Virgin and B. Andersson, Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim. Biophys. Acta, 1143 (1993) 113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.-M.1    Virgin, I.2    Andersson, B.3
  • 3
    • 0026547142 scopus 로고
    • Too much of a good thing: Light can be bad for photosynthesis
    • S. Barber and B. Andersson, Too much of a good thing: light can be bad for photosynthesis. Trends Biochem. Sci., 17 (1992) 61-66.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 61-66
    • Barber, S.1    Andersson, B.2
  • 4
    • 0026695796 scopus 로고
    • On the molecular mechanism of light-induced D1 protein degradation on photosystem II in core particles
    • A.H. Salter, B. Virgin, A. Hagman and B. Andersson, On the molecular mechanism of light-induced D1 protein degradation on photosystem II in core particles. Biochemistry, 31 (1992) 3990-3998.
    • (1992) Biochemistry , vol.31 , pp. 3990-3998
    • Salter, A.H.1    Virgin, B.2    Hagman, A.3    Andersson, B.4
  • 5
    • 0028578011 scopus 로고
    • Light-dependent degradation of the photosystem II D1 protein is retarded by inhibitors of chloroplast transcription and translation: Possible involvement of chloroplast encoded proteinase
    • H. Gong, Light-dependent degradation of the photosystem II D1 protein is retarded by inhibitors of chloroplast transcription and translation: possible involvement of chloroplast encoded proteinase. Biochim. Biophys. Acta, 1188 (1994) 422-426.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 422-426
    • Gong, H.1
  • 6
    • 0029088399 scopus 로고
    • B site and is dependent on protein synthesis
    • B site and is dependent on protein synthesis. Biochemistry, 34 (1995) 9625-9631.
    • (1995) Biochemistry , vol.34 , pp. 9625-9631
    • Komenda, J.1    Barber, J.2
  • 7
    • 0028112696 scopus 로고
    • Hypothesis on the control of D1 protein turnover by nuclear coded proteins in Chlamydomonas reinhardtii
    • E. Bracht and A. Trebst, Hypothesis on the control of D1 protein turnover by nuclear coded proteins in Chlamydomonas reinhardtii. Z. Naturforsch., 49c (1994) 439-446.
    • (1994) Z. Naturforsch. , vol.49 C , pp. 439-446
    • Bracht, E.1    Trebst, A.2
  • 8
    • 12044254041 scopus 로고
    • Photosystem II reaction center damage and repair in the green algae Dunaliella salina: Analysis under physiological and adverse irradiance conditions
    • J.H. Kim, J.A. Nemson and A. Melis, Photosystem II reaction center damage and repair in the green algae Dunaliella salina: analysis under physiological and adverse irradiance conditions. Plant Physiol., 103 (1993) 181-189.
    • (1993) Plant Physiol. , vol.103 , pp. 181-189
    • Kim, J.H.1    Nemson, J.A.2    Melis, A.3
  • 9
    • 0042775578 scopus 로고
    • Adenosine 3:5 cyclic monophosphate in Chlamydomonas reinhardtii: Isolation and characterisation
    • N. Amrhein and P. Fillner, Adenosine 3:5 cyclic monophosphate in Chlamydomonas reinhardtii: Isolation and characterisation. Proc. Natl. Acad. Sci., 70 (1973) 1099-1103.
    • (1973) Proc. Natl. Acad. Sci. , vol.70 , pp. 1099-1103
    • Amrhein, N.1    Fillner, P.2
  • 10
    • 0026045166 scopus 로고
    • Photosystem II particles from Chlamydomonas reinhardtii
    • C. de Vilry, B.A. Diner and J.-L. Popot, Photosystem II particles from Chlamydomonas reinhardtii. J. Biol. Chem., 266 (1991) 16614-16621.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16614-16621
    • De Vilry, C.1    Diner, B.A.2    Popot, J.-L.3
  • 11
    • 0001294420 scopus 로고
    • Regulation of protein metabolism: Coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membrane
    • A.K. Mattoo, H. Hoffmann-Falk, J.B. Marder and M. Edelman. Regulation of protein metabolism: coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membrane. Proc. Natl. Acad. Sci. USA, 81 (1984) 1380-1384.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1380-1384
    • Mattoo, A.K.1    Hoffmann-Falk, H.2    Marder, J.B.3    Edelman, M.4
  • 12
    • 0024979252 scopus 로고
    • Dynamics of the photosystem II reaction center
    • [12[ A.K. Mattoo, J.B. Marder and M. Edelman, Dynamics of the photosystem II reaction center. Cell, 56 (1989) 241-246.
    • (1989) Cell , vol.56 , pp. 241-246
    • Mattoo, A.K.1    Marder, J.B.2    Edelman, M.3
  • 13
    • 0001449340 scopus 로고
    • Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes
    • D.J. Kyle, I. Ohad and C.J. Arntzen, Membrane protein damage and repair: selective loss of a quinone-protein function in chloroplast membranes. Proc. Natl. Acad. Sci. USA, 81 (1984) 4070-4074.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4070-4074
    • Kyle, D.J.1    Ohad, I.2    Arntzen, C.J.3
  • 14
    • 0023429786 scopus 로고
    • Identification of a primary in vivo degradation product of the rapidly turning over 32 kDa protein of photosystem II
    • B.M. Greenberg, V. Gaba, A.K. Mattoo and M. Edelman, Identification of a primary in vivo degradation product of the rapidly turning over 32 kDa protein of photosystem II. EMBO J., 6 (1987) 2865-2869.
    • (1987) EMBO J. , vol.6 , pp. 2865-2869
    • Greenberg, B.M.1    Gaba, V.2    Mattoo, A.K.3    Edelman, M.4
  • 15
    • 0026043886 scopus 로고
    • Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: Evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem
    • C.A. Shipton and J. Barber, Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem. Proc. Natl. Acad. Sci. USA, 88 (1991) 6691-6695.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6691-6695
    • Shipton, C.A.1    Barber, J.2
  • 16
    • 0025919691 scopus 로고
    • B site by plastoquinone control the degradation of the D1 protein during photoinhibition in vivo
    • B site by plastoquinone control the degradation of the D1 protein during photoinhibition in vivo. J. Biol. Chem., 266 (1991) 21293-21299.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21293-21299
    • Gong, H.1    Ohad, I.2
  • 17
    • 0027426723 scopus 로고
    • Engagement of specific sites in the plastoquinone niche regulates degradation of the D1 protein in photosystem II
    • M.A.K. Jansen, B. Depka, A. Trebst and M. Edelman, Engagement of specific sites in the plastoquinone niche regulates degradation of the D1 protein in photosystem II J. Biol. Chem., 268 (1993) 21246-21252.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21246-21252
    • Jansen, M.A.K.1    Depka, B.2    Trebst, A.3    Edelman, M.4
  • 18
    • 0042274523 scopus 로고
    • A contact site between the two reaction center polypeptides of photosystem II is involved in photoinhibition
    • A. Trebst, A contact site between the two reaction center polypeptides of photosystem II is involved in photoinhibition. Z. Naturforsch., 46c (1991) 163-177.
    • (1991) Z. Naturforsch. , vol.46 C , pp. 163-177
    • Trebst, A.1
  • 19
    • 0025821441 scopus 로고
    • Apparent destabilisation of the SI-state related to herbicide resistance in a cyanobacterium mutant
    • D. Kirilovsky, J.M. Ducruet and A.-L. Etienne, Apparent destabilisation of the SI-state related to herbicide resistance in a cyanobacterium mutant. Biochim. Biophys. Acta, 1060 (1991) 37-44.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 37-44
    • Kirilovsky, D.1    Ducruet, J.M.2    Etienne, A.-L.3
  • 20
    • 0028079247 scopus 로고
    • S-1 destabilization and higher sensitivity to light in metribuzin resistant mutants
    • I. Perewoska, A.-L. Etienne, T. Miranda and D. Kirilovsky, S-1 destabilization and higher sensitivity to light in metribuzin resistant mutants. Plant Physiol., 104 (1994) 235-245.
    • (1994) Plant Physiol. , vol.104 , pp. 235-245
    • Perewoska, I.1    Etienne, A.-L.2    Miranda, T.3    Kirilovsky, D.4
  • 21
    • 0025323156 scopus 로고
    • Clp P represents a unique family of serine proteases
    • M.R. Maurizi, W.P. Clark, S.H. Kim and S. Gottesmann, Clp P represents a unique family of serine proteases. J. Biol. Chem., 265 (1990) 12546-12552.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12546-12552
    • Maurizi, M.R.1    Clark, W.P.2    Kim, S.H.3    Gottesmann, S.4
  • 22
    • 0001906342 scopus 로고
    • Redox control of gene expression and the function of chloroplast genomes- A hypothesis
    • J.F. Allen , Redox control of gene expression and the function of chloroplast genomes- a hypothesis. Photosynth. Res., 36 (1993) 95-102.
    • (1993) Photosynth. Res. , vol.36 , pp. 95-102
    • Allen, J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.