Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1832526 (PCC)
 5,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The rapid turn-over of the D1 polypeptide of the photosystem two complex has been suggested to be due to the presence of a "PEST"-like sequence located between putative transmembrane helices IV and V of D1 (Greenberg, B. M., Gaba, V., Mattoo, A. K. and Edelman, M. (1987) EMBO J. 6, 2865-2869). We have tested this hypothesis by constructing a deletion mutant (delta 226-233) of the cyanobacterium Synechocystis sp. PCC 6803 in which residues 226-233 of the D1 polypeptide, containing the PEST-like sequence, have been removed. The resulting mutant, delta PEST, is able to grow photoautotrophically and give light-saturated rates of oxygen at wild type levels. However electron transfer on the acceptor side of the complex is perturbed. Analysis of cells by thermoluminescence and by monitoring the decay in quantum yield of variable fluorescence following saturating flash excitation indicates that Q-B, but not Q-A, is destabilized in this mutant. Electron transfer on the donor side of photosystem two remains largely unchanged in the mutant. Turnover of the D1 polypeptide as examined by pulse-chase experiments using [35S]methionine was enhanced in the delta PEST mutant compared to strain TC31 which is the wild type control. We conclude that the PEST sequence is not absolutely required for turnover of the D1 polypeptide in vivo although deletion of residues 226-233 does have an effect on the redox equilibrium between QA and QB.
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PMID:Deletion of the PEST-like region of photosystem two modifies the QB-binding pocket but does not prevent rapid turnover of D1. 779 71

The degradation rate of the D1 polypeptide was measured in three Synechocystis PCC 6803 mutants in vivo. Mutations were introduced into a putative cleavage area of the D1 polypeptide (QEEET motif) and into the PEST-like area. PEST sequences are often found in proteins with a high turnover rate. The QEEET-motif mutants are CA1 [delta (E242-E244);Q241H] and E243K, and the third mutation, E229D, was directed to the PEST-like area. During high-light illumination (1500 mumol photons m-2 s-1) that induced photoinhibition of photosystem II (PSII), the half-life time of the D1 polypeptide in mutant E229D (t 1/2 = 35 min) was about twice as long as in AR (control strain) cells (t 1/2 = 19 min). In growth light (40 mumol photons m-2 s-1), the degradation rate of the D1 polypeptide in E229D and AR strains was the same (t 1/2 approximately 5 h). In growth light the D1 polypeptide was degraded faster in both QEEET-motif mutants than in the AR strain, but in photoinhibitory light the degradation rates were similar. According to these results, the highly conservative QEEET motif as such is not required for the proteolytic cut of the D1 polypeptide, but it does affect the rate of degradation. No simple correlation existed between the degradation rate of the D1 polypeptide and the susceptibility of PSII to photoinhibition in mutant and AR cells under our experimental conditions.
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PMID:Changes of amino acid sequence in PEST-like area and QEEET motif affect degradation rate of D1 polypeptide in photosystem II. 804 74

The sequence connecting alpha-helices D and E of the D1 protein in photosystem II (PSII) is longer than that found in the corresponding loop of the L subunit in the rhodobacterial reaction centre. This sequence was mutated in order to determine its role in oxygenic photosynthesis. Site-specific mutants, including point mutations and deletions of different size, of the PEST-like region and the putative cleavage area in the D-E loop of the D protein were constructed in Synechocystis sp. PCC 6803. The effects of mutations on the functional and structural properties of PSII and turnover of the D1 protein were examined. Our results demonstrate that deletion of either the PEST-like sequence (deltaR225-F239) or the putative cleavage region (deltaG240-V249, deltaR225-V249) of the D1 protein resulted in severe perturbations on the function of the QB electron acceptor of PSII. However, PSII centres of the mutant with deleted PEST region remained functional enough to support autotrophic growth whereas deletions of the putative cleavage region prevented autotrophic growth. Although enhanced degradation rates of the mutant D1 proteins under low-light growth conditions demonstrate that neither the PEST-like sequence nor the putative cleavage region are required for D1 proteolysis, it became clear that the extension in the D-E loop of the D1 protein is essential for proper PSII assembly and photoautotrophic growth. Moreover, modifications of the D-E loop resulted in transcriptional activation of the psbA gene, indicating that neither light intensity, as such, nor the activity of the electron transfer chain are the only determinants in regulation of psbA gene transcription.
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PMID:Mutagenesis of the D-E loop of photosystem II reaction centre protein D1. Function and assembly of photosystem II. 915 87