Skip to main content
SpringerLink
Log in

Prolonged high light treatment of plant cells results in changes of the amount, the localization and the electrophoretic behavior of several thylakoid membrane proteins

  • Regular Papers
  • Published:
Photosynthesis Research Aims and scope Submit manuscript

Abstract

The effect of a 30 h high light treatment on the amount and the localization of thylakoid proteins was analysed in low light grown photoautotrophic cells of Marchantia polymorpha and Chenopodium rubrum. High light treatment resulted in a net loss of D1 protein which was accompanied by comparable losses of other proteins of the PS II core (reaction center with inner antenna). LHC II proteins were not reduced correspondingly, indicating that these complexes are less affected by prolonged high light. High light influenced the distribution of PS II components between the grana and the stroma region of the thylakoid membrane, probably by translocation of the respective PS II proteins. Additionally, modifications of several thylakoid proteins were detected in high light treated cells of C. rubrum. These effects are discussed in relation to photoinhibitory damage and repair processes.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

BCA:

bioinchonic acid

chl:

chlorophyll

CF1 :

coupling factor

CYC:

cycloheximide

GT:

grana thylakoids

HL:

high light

LL:

low light

PAGE:

polyacrylamide gel electrophoresis

PFD:

photon flux density

PS I:

Photosystem I

PS II:

Photosystem II

RC:

reaction center

SDS:

sodium dodecylsulfate

ST:

stroma thylakoids

Thyl:

unfractionated thylakoids

References

  • Adir N, Shochat S and Ohad I (1990) Light-dependent D1 protein synthesis and translocation is regulated by reaction center II. J Biol Chem 265: 12563–12568

    Google Scholar 

  • Allen JF (1992) Protein phosphorylation in regulation of photosynthesis. Biochim Biophys Acta 1098: 275–335

    Google Scholar 

  • Anderson JM and Andersson B (1988) The dynamic photosynthetic membrane and regulation of solar energy conversion. Trends Biochem Sci 13: 351–355

    Google Scholar 

  • Anderson JM and Aro E-M (1994) Grana stacking and protection of Photosystem II in thylakoid membranes of higher plant leaves under sustained irradiance: An hypothesis. Photosynth Res 41: 315–326

    Google Scholar 

  • Aro E-M, Kettunen R and Tyystjärvi E (1992) ATP and light regulate D1 protein modification and degradation — role of the D1* in photoinhibition. FEBS Lett 297: 29–33

    Google Scholar 

  • Aro E-M, Virgin I and Andersson B (1993) Photoinhibition of Photosystem II. Inactivation, protein damage and turnover. Biochim Biophys Acta 1143: 113–134

    Google Scholar 

  • Barbato R, Friso G, Rigoni F, Dalla Vecchia F and Giacometti GM (1992) Structural changes and lateral redistribution of Photosystem II during donor side photoinhibition of thylakoids. J Cell Biol 119: 325–335

    Google Scholar 

  • Bergantino E, Dainese P, Cerovic Z, Sechi S and Bassi R (1995) A post-translational modification of the PS II subunit CP29 protects maize from cold stress. (submitted)

  • Callahan FE, Ghirardi ML, Sopory SK, Mehta AM Edelman M and Mattoo AK (1990) A novel metabolic form of the 32kDa-D1 protein in the grana-localized reaction center of Photosystem II. J Biol Chem 265: 15357–15360

    Google Scholar 

  • Demmig B, Cleland RE, Björkman O (1987) Photoinhibition, 77K chlorophyll fluorescence quenching and phosphorylation of the light-harvesting chlorophyll-protein complex of Photosystem II in soybean leaves. Planta 172: 378–385

    Google Scholar 

  • Dunbar BS and Schwoebel ED (1990) Preparation of polyclonal antibodies. In: Deutscher MP (ed) Methods in Enzymology, Vol 182, pp 663–670, Academic Press, San Diego

    Google Scholar 

  • Elich TD, Edelman M, Mattoo AK (1992) Identification, characterization, and resolution of the in vivo phosphorylated form of the PS II reaction center protein. J Biol Chem 267: 3523–3529

    Google Scholar 

  • Erickson JM, Rahire M, Malnoe P, Girard-Bascou J, Pierre Y, Bennoun P and Rochaix J-D (1986) Lack of the D2 protein in a Chlamydomonas reinhardtii psbD mutant affects Photosystem II stability and D1 expression. EMBO J 5: 1745–1754

    Google Scholar 

  • Godde D and Dannehl H (1994) Stress-induced chlorosis and increase in D1-protein turnover precede photoinhibition in spinach suffering under magnesium/sulphur deficiency. Planta 195: 291–300

    Google Scholar 

  • Hayden DB, Baker NR, Percival MP and Beckwith PB (1986) Modification of the Photosystem II light-harvesting chlorophyll a/b protein complex in maize during chill-induced photoinhibition. Biochim Biophys Acta 851: 86–92

    Google Scholar 

  • Hippler M, Ratajczak R and Haehnel W (1989) Identification of the plastocyanin binding subunit of Photosystem I. FEBS Lett 250: 280–284

    Google Scholar 

  • Hundal T, Virgin I, Styring S and Andersson B (1990) Changes in the organization of Photosystem II following light-induced D1-protein degradation. Biochim Biophys Acta 1017: 235–241

    Google Scholar 

  • Jansson S (1994) The light-harvesting chlorophyll a/b-binding proteins. Biochim Biophys Acta 1184: 1–19

    Google Scholar 

  • Kettunen R, Tyystjärvi E and Aro E-M (1991) D1 protein degradation during photoinhibition of intact leaves. FEBS Lett 290: 153–156

    Google Scholar 

  • Kim JH, Glick RE and Melis A (1993) Dynamics of photosystem stoichiometry adjustment by light quality in chloroplasts. Plant Physiol 102: 181–190

    Google Scholar 

  • Krause GH (1988) Photoinhibition of photosynthesis. An evaluation of damaging and protective mechanisms. Physiol Plant 74: 566–574

    Google Scholar 

  • Leto KJ, Bell E and Mc Intosh L (1985) Nuclear mutation leads to an accelerated turnover of chloroplast encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking Photosystem II. EMBO J 4: 1645–1653

    Google Scholar 

  • Makino A and Osmond B (1991) Solubilization of ribulose-1,5-bisphosphate carboxylase from the membrane fraction of pea leaves. Photosynth Res 29: 79–85

    Google Scholar 

  • Mattoo AK and Edelman M (1987) Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein. Proc Natl Acad Sci USA 84: 1497–1501

    Google Scholar 

  • Ohad I, Kyle DJ and Arntzen CJ (1984) Membrane protein damage and repair: removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes. J Cell Biol 99: 481–485

    Google Scholar 

  • Öquist G, Anderson JM, Mc Caffery S and Chow WS (1992) Mechanistic differences in photoinhibition of sun and shade plants. Planta 188: 422–431

    Google Scholar 

  • Ottander C, Hundal T, Andersson B, Huner NPA and Öquist G (1993) Photosystem II reaction centers stay intact during low temperature photoinhibition. Photosynth Res 35: 191–200

    Google Scholar 

  • Porra RJ, Thompson WA and Kriedemann PE (1989) Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim Biophys Acta 975: 384–394

    Google Scholar 

  • Rintamäki E, Salo R and Aro E-M (1994) Rapid turnover of the D1 reaction-center protein of Photosystem II as a protective mechanism against photoinhibition in a moss, Ceratodon purpureus (Hedw.) Brid. Planta 193: 520–529

    Google Scholar 

  • Schäfer C (1994) Controlling the effects of excessive light energy fluxes: dissipative mechanisms, repair processes, and long-term acclimation. In: Schulze E-D (ed) Flux Control in Biological Systems, pp 37–54. Academic Press, San Diego

    Google Scholar 

  • Schäfer C and Schmid V (1995) The use of photoautotrophic plant cells as a model system in studies on light stress and photoinhibition. In: Chagvardieff P, Nato A, Carré F (eds) Proceedings of the International Symposium ‘Ecophysiology and photosynthetic in vitro cultures’ (in press)

  • Schäfer C, Schmid V and Roos M (1994) Characterization of high-light-induced increases in xanthophyll cycle pigment and lutein contents in photoautotrophic cell cultures. J Photochem Photobiol B 22: 67–75

    Google Scholar 

  • Schäfer C and Schmidt E (1991) Light acclimation potential and xanthophyll cycle pigments in photoautotrophic suspension cells of Chenopodium rubrum. Physiol. Plant. 82: 440–448

    Google Scholar 

  • Schäfer C, Vogg G and Schmid V (1993) Evidence for loss of D1 protein during photoinhibition of Chenopodium rubrum L. culture cells. Planta 189: 433–439

    Google Scholar 

  • Schmid V (1995) Lichtstreßbedingte Änderungen in der Menge, der Verteilung und im Umsatz photosynthetischer Pigment-Protein-Komplexe bei photoautotrophen Chenopodium rubrum Suspensionskulturzellen. Shaker Verlag, Aachen

    Google Scholar 

  • Schmid V and Schäfer C (1994) Alterations of the chlorophyll-protein pattern in chronically photoinhibited Chenopodium rubrum cells. Planta 192: 473–479

    Google Scholar 

  • Schnettger B, Critchley C, Santore UJ, Graf M and Krause GH (1994) Relationship between photoinhibition of photosynthesis, D1 protein turnover and chloroplast structure: Effects of protein synthesis inhibitors. Plant Cell Environ 17: 55–64

    Google Scholar 

  • Schuster G, Timberg R and Ohad I (1988) Turnover of thylakoid Photosystem II proteins during photoinhibition of Chlamydomonas reinhardtii. Eur J Biochem 177: 403–410

    Google Scholar 

  • Smith PK, Krohn RI, Hermanson AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ and Klenk DC (1985) Measurement of protein using Bicinchonic acid. Anal Biochem 150: 76–85

    Google Scholar 

  • Wynn MR and Malkin R (1988) Interaction of plastocyanin with Photosystem I: A chemical cross-linking study of the polypeptide that binds plastocyanin. Biochemistry 27: 5863–5869

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Lehrstuhl Pflanzenphysiologie, Universität Bayreuth, Universitätsstraße 30, 95440, Bayreuth, Germany

    Volkmar Schmid, Stefan Peter & Christian Schäfer

Authors
  1. Volkmar Schmid
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Stefan Peter
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Christian Schäfer
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Schmid, V., Peter, S. & Schäfer, C. Prolonged high light treatment of plant cells results in changes of the amount, the localization and the electrophoretic behavior of several thylakoid membrane proteins. Photosynth Res 44, 287–295 (1995). https://doi.org/10.1007/BF00048602

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00048602

Key words

Search

Navigation