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  • 1
    Electronic Resource
    Electronic Resource
    Degradation of the D1- and D2-Proteins of Photosystem II in Higher Plants Is Regulated by Reversible Phosphorylation (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 16022-16029 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00049a016
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  • 2
    Electronic Resource
    Electronic Resource
    Lateral diffusion of an integral membrane protein: Monte Carlo analysis of the migration of phosphorylated light-harvesting complex II in the thylakoid membrane (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 11915-11922 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00095a022
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  • 3
    Electronic Resource
    Electronic Resource
    The PSII-S Protein of Higher Plants: A New Type of Pigment-Binding Protein (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 11133-11141 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00035a019
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  • 4
    Electronic Resource
    Electronic Resource
    On the molecular mechanism of light-induced D1 protein degradation in photosystem II core particles (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 3990-3998 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00131a014
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  • 5
    Electronic Resource
    Electronic Resource
    Light-induced changes of photosystem II activity in dark-grown Scots pine seedlings (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 84 (1992), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Both chlorophyll a and b and polypeptides of the photosynthetic apparatus are found in gymnosperm seedlings. germinated and grown in absolute darkness. The photosystem II (PSII) activity is, however, limited, probably due to an inactive oxygen evolving system. In the present study dark-grown seedlings of Scots pine (Pinus sylvestris L.) were transferred to light and changes in antenna size and the activation process of PSII were investigated using fluorescence measurements and quantitative western blotting. It was found that the activation process is rapid, requires very little light and that strong light inhibits the process. It takes place without any changes in the primary reactions of PSII. Furthermore, all polypeptides except the major light-harvesting chlorophyll a/b-binding protein complex of PSII (LHCII) were present in dark-grown seedlings in amounts comparable to the light treated control. The dark-grown seedlings had the same LHCII polypeptide composition as light treated seedlings, and the LHCII present seemed to be fully connected to the reaction centre. The results indicate that activation of PSII in dark-grown conifer seedlings resembles the photoactivation process of angiosperms. This implies that the fundamental processes in the assembly of the photosystem II complex is the same in all plants, but that the regulation differs between different taxa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1992.tb08757.x
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  • 6
    Electronic Resource
    Electronic Resource
    A convenient and versatile hydroponic cultivation system for Arabidopsis thaliana (2004)
    Oxford, UK; Malden, USA : Munksgaard International Publishers
    Physiologia plantarum 121 (2004), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A versatile two-step cultivation procedure for Arabidopsis thaliana is described for the production of large quantities of leaf material suitable for biochemical and biophysical analysis. The first step comprises a miniature greenhouse made out of a plastic pipette box to grow the seedlings to the six-leaf stage. For continued growth, the seedlings are transferred to hydroponic cultivation using an opaque container covered by a styrofoam lid. Transfer of the small seedlings to hydroponic culture is facilitated by growth in separate pipette tips, which protects vulnerable roots from damage. The hydroponic cultivation system is easy to scale-up and produces large amounts of relatively large leaves and roots. This hydroponic system produces enough plant material to make Arabidopsis a feasible model for biochemical and biophysical experiments, which can be combined with the available genetic information to address various aspects of plant functional genomics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0031-9317.2004.00350.x
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  • 7
    Electronic Resource
    Electronic Resource
    Proteolytic activities and proteases of plant chloroplasts (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 100 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A concise overview on the current knowledge of the proteolytic activities in chloroplasts is presented, with an emphasis on the proteolytic events associated with thylakoid membranes. The Dl reaction centre protein of photosystem II undergoes rapid light-dependent turnover and chlorophyll a/b-binding proteins are effectively degraded upon acclimation of plants to higher irradiances. Insights into the partially characterized proteolytic systems in each case will be presented, but the proteases involved still remain unknown. It can be envisaged, however, that the proteolysis is probably an as highly regulated phenomenon as the various steps during biosynthesis of the photosynthetic multiprotein complexes. From the protease point of view, more progress has recently been made in characterization of processing proteases involved in protein import into chloroplasts and in C-terminal processing of the Dl protein. Moreover, there are an increasing number of proteases in chloroplasts which have been discovered and identified as bacterial homologues. These include a Clp-type protease, a homologue of the bacterial protease FtsH and the cyanobacterial PcrA protease, all of which have a specific location in the chloroplast but their definite physiological substrates are still missing. Attempts are made to bring together the recent progress in the identification of proteases and characterisation of proteolytic events in chloroplasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb00005.x
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  • 8
    Electronic Resource
    Electronic Resource
    Inside-out thylakoid vesicles. An important tool for the characterization of the photosynthetic membrane (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 65 (1985), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1985.tb02403.x
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  • 9
    Electronic Resource
    Electronic Resource
    Rapid isolation of photosystem I chlorophyll-binding proteins by anion exchange perfusion chromatography (1995)
    Springer
    Photosynthesis research 45 (1995), S. 41-49 
    Details
    ISSN: 1573-5079
    Keywords: fluorescence ; LHC I-680 ; LHC I-730 ; light-harvesting complex I (LHC I) ; PS I
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract With the new method of anion exchange perfusion chromatography we have devised an extremely rapid technique to subfractionate spinach Photosystem I into its chlorophyll a containing core complex and various components of the Photosystem I light-harvesting antenna (LHC I). The isolation time for the LHC I subcomplexes following solubilisation of native Photosystem I was reduced from 50 h using traditional density centrifugation procedures down to only 10–25 min by perfusion chromatography. Within this very short period of isolation, LHC I has been obtained as subfractions highly enriched in Lhca2+3 (LHC I-680) and Lhca1+4 (LHC I-730). Moreover, other highly enriched subfractions of LHC I such as Lhca2, Lhca3 and Lhca1+2+4 were obtained where the later two populations have not previously been obtained in a soluble form and without the use of SDS. These various subfractions of the LHC I antenna have been characterised by absorption spectroscopy, 77 K fluorescence-spectroscopy and SDS-PAGE demonstrating their identities, functional intactness and purity. Furthermore, the analyses located a chlorophyll b pool to preferentially transfer its excitation energy to the low energy F735 chromophore, and located specifically the origin of the 730 nm fluorescence to the Lhca4 component. It was also revealed that Lhca2 and Lhca3 have identical light-harvesting properties. The isolated Photosystem I core complex showed high electron transport capacity (1535 μmoles O2 mg Chl−1 h−1) and low fluorescence yield (0.4%) demonstrating its high functional integrity. The very rapid isolation procedure based upon perfusion chromatography should in a significant way facilitate the subfractionation of Photosystem I proteins and thereby allow more accurate functional and structural studies of individual components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00032234
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  • 10
    Electronic Resource
    Electronic Resource
    Expression of ELIPs and PS II-S protein in spinach during acclimative reduction of the Photosystem II antenna in response to increased light intensities (1997)
    Springer
    Photosynthesis research 54 (1997), S. 227-236 
    Details
    ISSN: 1573-5079
    Keywords: chlorophyll ; early light-inducible protein ; light acclimation ; light-harvesting complex ; photoinhibition ; thylakoid proteases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The PS II-S protein and the so-called early light-inducible proteins (ELIPs) are homologous to the chlorophyll a/b-binding (Cab) gene products functioning in light-harvesting. The functional significance of these two CAB homologues is not known although they have been considered to bind pigments and in the case of the PS II–S protein this has been experimentally supported. The role of these two proteins does not appear to be light-harvesting but instead they are suggested to play a role as quenchers of free chlorophyll molecules during biogenesis and/or degradation of pigment-binding proteins. Such a role would be essential to eliminate the toxic and damaging effects that can be induced by free chlorophyll in the light. To this end the expression and characteristics of the ELIPs and the PS II–S protein were investigated in spinach leaves acclimating from low to high light intensities. Under these conditions there is a reduction in the antenna size of Photosystem II due to proteolytic digestion of its major chlorophyll a/b-binding protein (LHC II). During this acclimative proteolysis, up to one third of LHC II can be degraded and consequently substantial amounts of chlorophyll molecules will lose their binding sites. Our results reveal that there is a close correlation between ELIP accumulation and the onset of the LHC II degradation as low light-grown spinach leaves are subjected to increased light intensities. In contrast, there was no change in the relative level of the PS II–S protein during the acclimation process. It is concluded that the role for the ELIPs may be related to binding of liberated chlorophyll molecules and quenching of the toxic effects during LHC II degradation. In addition it was shown that in spinach four different ELIP species can be expressed and that they show different accumulation patterns in response to increased light intensities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005920730947
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