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1.
Plant Cell Physiol ; 41(9): 1045-54, 2000 Sep.
Article in English | MEDLINE | ID: mdl-11100777

ABSTRACT

Plants respond to changing light conditions by altering the stoichiometry between components of the photosynthetic electron transport chain of chloroplast thylakoids. We measured specific run-on transcription of the chloroplast genes psaB, psbA and rbcL in pea (Pisum sativum L.) seedlings grown under three different conditions of illumination: light selective for photosystem I (PSI-light); light selective for photosystem II (PSII-light); and a combination of PSI- and PSII-light (mixed light, ML). The transcriptional rate of the psaB gene increased under PSII-light and decreased under PSI-light, while the transcriptional rates of the psbA and rbcL genes were affected only in a non-specific way. Similar effects also occurred in plants grown under ML and switched to either PSI- or PSII-light for 4 h. Addition of the inhibitors of photosynthetic electron transport 3-(3,4 dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) influenced psaB transcription in isolated, illuminated chloroplasts: DCMU addition resulted in oxidation of the plastoquinone pool and decreased transcription of psaB; DBMIB addition resulted in reduction of the plastoquinone pool and increased transcription of psaB. The experimental results obtained in vivo and in vitro provide evidence for coupling between the redox state of plastoquinone and the rate of transcription of the psaB gene in pea.


Subject(s)
Chloroplasts/metabolism , Gene Expression Regulation, Plant , Membrane Proteins/genetics , Photosynthesis , Photosynthetic Reaction Center Complex Proteins/genetics , Photosystem I Protein Complex , Pisum sativum/genetics , Pisum sativum/metabolism , Plastoquinone/metabolism , Ribulose-Bisphosphate Carboxylase , Transcription, Genetic , Dibromothymoquinone/pharmacology , Diuron/pharmacology , Electron Transport , Gene Expression Regulation, Plant/drug effects , Kinetics , Light , Oxidation-Reduction , Photosystem II Protein Complex , Plant Proteins/genetics , Transcription, Genetic/drug effects
2.
IUBMB Life ; 48(3): 271-6, 1999 Sep.
Article in English | MEDLINE | ID: mdl-10690637

ABSTRACT

Two photosystems, I and II, absorb and convert light energy in photosynthesis in chloroplasts of green plants. The genes psbA and psaAB of the cytoplasmic chloroplast genome encode core components of photosystem II and photosystem I, respectively. Here we show that the absolute amounts of photosystem I and photosystem II respond, in a complementary manner, to changes in light quality that preferentially excite each photosystem in mustard seedlings. We also show that the initial response to altered energy distribution is a change in the rates of transcription of psbA and psaAB. Changes in chlorophyll fluorescence emission in vivo suggest that the signal initiating this change is the oxidation-reduction state of plastoquinone, a component of the photosynthetic electron transport chain that connects photosystem I and photosystem II. The results are consistent with transcriptional effects observed previously with chloroplasts isolated in vitro and demonstrate that redox control of chloroplast transcription initiates long-term adjustments that compensate for imbalance in energy distribution and adapt the whole plant to altered light environments.


Subject(s)
Chloroplasts/physiology , Gene Expression Regulation, Plant/physiology , Light-Harvesting Protein Complexes , Photosynthesis/genetics , Photosynthetic Reaction Center Complex Proteins/genetics , Photosystem I Protein Complex , Plant Physiological Phenomena , Plant Proteins/genetics , Light , Photosystem II Protein Complex , Transcription, Genetic
3.
Biochem Biophys Res Commun ; 250(3): 617-22, 1998 Sep 29.
Article in English | MEDLINE | ID: mdl-9784395

ABSTRACT

Phosphorylation of chloroplast thylakoid proteins, in particular light harvesting complex II (LHC II), is believed to play an important role in regulating photosynthetic electron transfer. Evidence supporting the involvement of multiple protein kinases in this system is mounting. We have re-examined pea thylakoid membranes and found evidence for a membrane-associated protein tyrosine kinase (PTK). Phosphorylation of many thylakoid proteins, including LHC II, is sensitive to treatment with the tyrosine kinase inhibitor genistein. Anti-phosphotyrosine antibodies react specifically with nine thylakoid proteins, two of which have been identified as components of LHC II. The phosphate associated with these two proteins is also resistant to strong base and acid treatment, further substantiating the assignment of phosphotyrosine. Potential interactions between this novel chloroplast PTK activity and the well-documented threonine kinase activities are discussed and the presence of a cascade of thylakoid protein kinases is proposed.


Subject(s)
Chloroplasts/metabolism , Photosynthetic Reaction Center Complex Proteins/metabolism , Plant Proteins/metabolism , Protein-Tyrosine Kinases/metabolism , Phosphorylation
4.
Scand J Dent Res ; 94(2): 164-73, 1986 Apr.
Article in English | MEDLINE | ID: mdl-3458287

ABSTRACT

In the present study a powerful method for measuring adhesion is introduced. It is based on the observation that the bacterial layer is usually capable of maintaining an interior pressure, but fractures when this pressure exceeds a certain critical value characteristic of the mechanical and adhesive properties of each specific bacteria and its formed matrix. A water jet from a nozzle was directed on the bacterial layer of the specimen. A specimen covered with a layer of Streptococcus mutans, grown in an artificial mouth, was placed on a sledge and displaced twice, at constant speed in front of the jet, thus forming two grooves in the plaque layer. When the grooves are made in parallel utilizing different water pressures, the critical pressure for causing disengagement of the plaque, pc, can be evaluated. It is claimed that pc gives an estimate of the plaque adhesion. Polished and ground surfaces of four materials were investigated, namely amalgam, PMMA, gold and porcelain-coated gold.


Subject(s)
Bacterial Physiological Phenomena , Dental Materials , Dental Restoration, Permanent , Adhesiveness , Chemical Phenomena , Chemistry, Physical , Dental Alloys , Dental Amalgam , Dental Porcelain , Gold Alloys , Humans , Methylmethacrylates , Models, Biological , Mouth , Surface Properties
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