Skip to main content
Log in

Energy transfer for low temperature fluorescence in PS II mutant thylakoids

  • Light-Harvesting Complexes
  • Regular Paper
  • Published:
Photosynthesis Research Aims and scope Submit manuscript

Abstract

The Chl-protein complexes of three maize (Zea mays L.) mutants and one barley (Hordeum vulgare L.) mutant were analyzed using low temperature Chl fluorescence emissions spectroscopy and LDS-polyacrylamide gel electrophoresis. The maize mutants hcf-3, hcf-19, and hcf-114 all exhibited a high Chl fluorescence (hcf) phenotype indicating a disruption of the energy transfer within the photosynthetic apparatus. The mutations in each of these maize mutants affects Photosystem II. The barley mutant analyzed was the well characterized Chl b-less mutant chlorina-f2, which did not exhibit the hcf phenotype. Chlorina-f2 was used because no complete Chl b-less mutant of maize is available. Analysis of hcf-3, hcf-19, and hcf-114 revealed that in the absence of CP43, LHC II can still transfer excitation energy to CP47. These results suggest that in mutant membranes LHC II can interact with CP47 as well as CP43. This functional interaction of LHC II with CP47 may only occur in the absence of CP43, however, it is possible that LHC II is positioned in the thylakoid membranes in a manner which allows association with both CP43 and CP47.

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

Access this article

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

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

hcf :

high chlorophyll fluorescence

LDS:

lithium dodecyl sulfate

LHC II:

light-harvesting complex of Photosystem II

LHC I:

light-harvesting complex of Photosystem I

CPIa:

chlorophyll-protein complex consisting of LHC I and the PS I core complex

CPI:

chlorophyll-protein complex consisting of the PS I core complex

CP47:

47 kDa chlorophyll-protein of the Photosystem II core

CP43:

43 kDa chlorophyll-protein of the Photosystem II core

CP29:

29 kDa chlorophyll-protein of Photosystem II

CP26:

26 kDa chlorophyll-protein of Photosystem II

CP24:

24 kDa chlorophyll-protein of Photosystem II

fp:

free pigments

References

  • Arnon DI (1949) Copper enzymes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris. Plant Physiol 24: 1–15

    Google Scholar 

  • Bassi R and Simpson DJ (1987a) Chlorophyll-protein complexes of barley Photosystem I. Eur J Biochem 163: 221–230

    Google Scholar 

  • Bassi R, Høyer-Hanson G, Barbato R, Giacometti GM and Simpson DJ (1987b) Chlorophyll-proteins of the Photosystem II antenna system. J Biol Chem 202: 13333–13342

    Google Scholar 

  • Bricker TM (1990) The structure and function of CPa-1 and CPa-2 in Photosystem II. Photosynth Res 24: 1–13

    Google Scholar 

  • Camm EL and Green BL (1980) Fractionation of thylakoid membranes with the nonionic detergent octyl-β-d-glucopyranoside. Plant Physiol 66: 428–432

    Google Scholar 

  • Cook WB and Miles D (1992) Nuclear mutations affecting plastoquinone accumulation in maize. Photosynth Res 31: 99–111

    Google Scholar 

  • Delepelaire P and Chua N-H (1979) Lithium dodecyl sulfate/polyacrylamide gel electrophoresis of thylakoid membranes at 4 degrees C: Characterization of two additional chlorophyll a-protein complexes. Proc Natl Acad Sci USA 76: 111–115

    Google Scholar 

  • Dreyfuss BW and Thornber JP (1994a) Assembly of the light-harvesting complexes (LHCs) of Photosystem II. Plant Physiol 106: 829–839

    Google Scholar 

  • Dreyfuss BW and Thornber JP (1994b) Organization of the light-harvesting complex of Photosystem I and its assembly during plastid development. Plant Physiol 106: 841–848

    Google Scholar 

  • Dunahay TG and Staehelin LA (1986) Isolation and characterization of a new minor chlorophyll a/b-protein complex (CP24) of spinach. Plant Physiol 80: 429–434

    Google Scholar 

  • Goldbeck JH and Bryant DA (1991) Photosystem I. In: Lee CP (ed) Current Topics in Bioenergetics, pp 83–177. Academic Press, New York

    Google Scholar 

  • Green BL (1988) The chlorophyll-protein complexes of higher plant photosynthetic membranes or just what green band is that? Photosynth Res 15: 3–32

    Google Scholar 

  • Highkin HR (1950) Chlorophyll studies on barley mutants. Plant Physiol 25: 294–306

    Google Scholar 

  • Ikeuchi M, Hirano A and Inoue Y (1991) Correspondence of apoproteins of light-harvesting chlorophyll a/b complexes associated with Photosystem I to cab genes: Evidence for a novel type-IV apoprotein. Plant Cell Physiol 32: 103–112

    Google Scholar 

  • Krause GH and Weis E (1991) Chlorophyll fluorescence and photosynthesis: The basics. Annu Rev Plant Physiol 42: 313–49

    Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685

    Google Scholar 

  • Leto K and Arntzen CJ (1981) Cation-mediated regulation of excitation energy distribution in chloroplasts lacking organized Photosystem II complexes. Biochim Biophys Acta 637: 107–117

    Google Scholar 

  • Leto K and Miles D (1980) Characterization of three Photosystem II mutants in Zea mays L. lacking a 32,000 dalton lamellar polypeptide. Plant Physiol 66: 18–24

    Google Scholar 

  • Machold O, Simpson DJ and Møller BL (1979) Chlorophyll-proteins of thylakoids from wild-type and mutant barley (Hordeum vulgare L.). Carlsberg Res Commun 44: 235–254

    Google Scholar 

  • Markwell JP, Thornber JP and Boggs RT (1979) Higher plant chloroplasts: Evidence that all the chlorophyll exists as chlorophyll-protein complexes. Proc Natl Acad Sci 76: 1233–1235

    Google Scholar 

  • Metz JG and Miles D (1982) Use of nuclear mutants of maize to identify components of Photosystem II. Biochim Biophys Acta 681: 95–102

    Google Scholar 

  • Miles D (1980) Photosynthetic mutants of higher plants: Maize. In: San Pietro A (eds) Methods in Enzymology, Photosynthesis Part C, Vol 69, pp 1–23. Academic Press New York

    Google Scholar 

  • Miles D (1982) The use of mutations to probe photosynthesis in higher plants. In: Edelman M, Hallick RB and Chua N-H (eds) Methods in Chloroplast Molecular Biology, pp 75–107, Elsevier, Amsterdam

    Google Scholar 

  • Murata N and Satoh K (1986) Absorption and fluorescence emission by intact cells, chloroplasts, and chlorophyll-protein complexes. In: Govindjee, Amesz J and Fork DC (eds) Light Emissions by Plants and Bacteria, pp 137–159. Academic Press, New York

    Google Scholar 

  • Peter GF and Thornber JP (1991) Biochemical composition and organization of higher plant Photosystem II light-harvesting pigment-proteins. J Biol Chem 266: 16745–16754

    Google Scholar 

  • Robertson DW (1937) Inheritance in barley, II. Genetics 22: 443–451

    Google Scholar 

  • Siefermann-Harms D (1988) Fluorescence properties of isolated chlorophyll-protein complexes. In: Lichtenthaler HK (ed) Chl Fluorescence, pp 45–54. Kluwer Academic Publishers, Dordrecht

    Google Scholar 

  • Thornber JP (1975) Chlorophyll-proteins: Light-harvesting and reaction center components of plants. Ann Rev Plant Physiol 26: 127–158

    Google Scholar 

  • Thornber JP (1986) Biochemical characterization and structure or pigment-proteins of photosynthetic organisms. In. Encyclopedia of Plant Physiology, Vol 19, pp 98–142. Springer-Verlag, Berlin/Heidelberg

    Google Scholar 

  • Thornber JP, Gregory RPF, Smith CA and Baily JL (1967) Studies on the nature of the chloroplast lamella. I. Preparation and some properties of two chlorophyll-protein complexes. Biochemistry 6: 391–396

    Google Scholar 

  • Thornber JP and Highkin HR (1974) Composition of the photosynthetic apparatus of normal barley leaves and a mutant lacking chlorophyll b. Eur J Biochem 41: 109–116

    Google Scholar 

  • Zilber AL and Malkin R (1992) Organization and topology of photosystem I subunits. Plant Physiol 99: 901–911

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Krugh, B.W., Miles, D. Energy transfer for low temperature fluorescence in PS II mutant thylakoids. Photosynth Res 44, 117–125 (1995). https://doi.org/10.1007/BF00018302

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00018302

Key words

Navigation