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  • 1
    Electronic Resource
    Electronic Resource
    phrA, the major photoreactivating factor in the cyanobacterium Synechocystis sp. strain PCC 6803 codes for a cyclobutane-pyrimidine-dimer-specific DNA photolyase (2000)
    Springer
    Archives of microbiology 173 (2000), S. 412-417 
    Details
    ISSN: 1432-072X
    Keywords: Synechocystis sp. strain PCC 6803 phrA DNA photolyase Cyclobutane pyrimidine dimer Over-expression plasmid pSL1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. A new broad-host-range plasmid, pSL1211, was constructed for the over-expression of genes in Synechocystis sp. strain PCC 6803. The plasmid was derived from RSF1010 and an Escherichia coli over-expression plasmid, pTrcHisC. Over-expressed protein is made with a removable N-terminal histidine tag. The plasmid was used to over-express the phrA gene and purify the gene product from Synechocystis sp. strain PCC 6803. PhrA is the major ultraviolet-light-resistant factor in the cyanobacterium. The purified PhrA protein exhibited an optical absorption spectrum similar to that of the cyclobutane pyrimidine dimer (CPD) DNA photolyase from Synechococcus sp. strain PCC 6301 (Anacystis nidulans). Mass spectrometry analysis of PhrA indicated that the protein contains 8-hydroxy-5-deazariboflavin and flavin adenine dinucleotide (FADH2) as cofactors. PhrA repairs only cyclobutane pyrimidine dimer but not pyrimidine (6-4) pyrimidinone photoproducts. On the basis of these results, the PhrA protein is classified as a class I, HDF-type, CPD DNA photolyase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030000164
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  • 2
    Electronic Resource
    Electronic Resource
    Targeted interruption of the psaA and psaB genes encoding the reaction-centre proteins of photosystem I in the filamentous cyanobacterium Anabaena variabilis ATCC 29413 (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 9 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The two reaction-centre proteins of the photosystem I (PSI) complex are encoded by two adjacent genes named psaA and psaB. We have performed targeted mutagenesis to insertionally inactivate each of these genes in the filamentous cyanobacterium Anabaena variabilis ATCC 29413. The resulting mutant strains, termed psaA:: NmR and psaB:: NmR, were blue because of a high ratio of phycobilin to chlorophyll and were unable to grow in light. These mutant cells also lacked chemically reducible P700 (the reaction-centre chlorophylls of PSI) and as a consequence did not exhibit any PSI-mediated photochemical activity. However, their photosystem II (PSII) complexes were fully active. The loss of the PsaA and PsaB proteins and their associated chlorophyll molecules resulted in a five- to sevenfold decrease in the chlorophyll/PSII ratio in the mutant cells relative to the wild-type cells. Interestingly, the psaS:: NmR and not the psaA:: NmR mutant strain retained a small fluorescence peak (77K) at 721 nm originating from chlorophyll molecule(s) presumably bound to a small amount of the PsaA protein present in the psaB mutant. These results demonstrate that this organism is suitable for the manipulation of PSI reaction-centre proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01227.x
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  • 3
    Electronic Resource
    Electronic Resource
    The D1 protein of the photosystem II reaction-centre complex accumulates in the absence of D2: analysis of a mutant of the cyanobacterium Synechocystis sp. PCC 6803 lacking cytochrome d559 (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The reaction center core of photosystem II, a multi-protein membrane bound complex, is composed of a heterodimer of two proteins, D1 and D2. A random mutagenesis technique was used to isolate a photosystem II deficient mutant, CP6t16, of the unicellular cyanobacterium, Synechocystis sp. PCC 6803. Nucleotide sequence analysis showed that the primary lesion in CP6t16 is an ochre mutation introducing a translational stop codon in the psbE gene, encoding the α-subunit of cytochrome b 559, an integral component of the PSII complex. Analysis of the protein composition of CP6t16 thylakoid membranes isolated in the presence of serine protease inhibitors revealed that, in the absence of cytochrome b 559, the D2 protein is also absent. However, the D1 protein is stably incorporated in these membranes, suggesting that the synthesis and integration of D1 are independent of those of D2 and cytochrome 6559.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb01544.x
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  • 4
    Electronic Resource
    Electronic Resource
    Presence of an N-terminal presequence in the PsaI protein of the Photosystem I complex in the filamentous cyanobacterium Anabaena variabilis ATCC 29413 (1992)
    Springer
    Plant molecular biology 20 (1992), S. 987-990 
    Details
    ISSN: 1573-5028
    Keywords: Anabaena ; cyanobacteria ; N-terminal processing ; Photosystem I
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The psaI gene encoding the 5.2 kDa protein component (PsaI) of the photosystem I complex was cloned from the cyanobacterium Anabaena 29413. The gene is present in single copy in this cyanobacterial genome. The nucleotide sequence of a 500 bp region of the cloned DNA revealed the presence of an open reading frame encoding a 46 amino acid long polypeptide. The N-terminal 11 residues are absent in the mature polypeptide and thus represents the first identified cleavable presequence on the PsaI protein. We suggest that this presequence directs the N-terminus of the protein to the thylakoid lumen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00027168
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  • 5
    Electronic Resource
    Electronic Resource
    The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range (1999)
    Springer
    Plant molecular biology 40 (1999), S. 37-44 
    Details
    ISSN: 1573-5028
    Keywords: copper ; iron ; manganese ; metal transport ; plant root ; zinc
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The molecular basis for the transport of manganese across membranes in plant cells is poorly understood. We have found that IRT1, an Arabidopsis thaliana metal ion transporter, can complement a mutant Saccharomyces cerevisiae strain defective in high-affinity manganese uptake (smf1Δ). The IRT1 protein has previously been identified as an iron transporter. The current studies demonstrated that IRT1, when expressed in yeast, can transport manganese as well. This manganese uptake activity was inhibited by cadmium, iron(II) and zinc, suggesting that IRT1 can transport these metals. The IRT1 cDNA also complements a zinc uptake-deficient yeast mutant strain (zrt1zrt2), and IRT1-dependent zinc transport in yeast cells is inhibited by cadmium, copper, cobalt and iron(III). However, IRT1 did not complement a copper uptake-deficient yeast mutant (ctr1), implying that this transporter is not involved in the uptake of copper in plant cells. The expression of IRT1 is enhanced in A. thaliana plants grown under iron deficiency. Under these conditions, there were increased levels of root-associated manganese, zinc and cobalt, suggesting that, in addition to iron, IRT1 mediates uptake of these metals into plant cells. Taken together, these data indicate that the IRT1 protein is a broad-range metal ion transporter in plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026438615520
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  • 6
    Electronic Resource
    Electronic Resource
    An unusual organization of the genes encoding cytochrome b 559 in Chlamydomonas reinhardtii: psbE and psbF genes are separately transcribed from different regions of the plastid chromosome (1995)
    Springer
    Molecular genetics and genomics 246 (1995), S. 600-604 
    Details
    ISSN: 1617-4623
    Keywords: Cytochrome b 559 ; Photosystem II Chloroplast gene expression ; Chlamydomonas reinhardtii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The psbE and psbF genes encode the apoproteins of cytochrome b 559, an essential component of the pigment protein complex photosystem II. Together with psbL and psbJ, these genes constitute a single operon in all photosynthetic organisms examined thus far. We have cloned and sequenced the psbE and psbF genes of the Chlamydomonas reinhardtii plastid genome. The predicted amino-terminal domains of both polypeptides are more basic than those of other organisms, and the sequence of the psbE gene product indicates a departure from the ‘positive-inside’ rule for the insertion of proteins in the thylakoid membrane. Northern blot analysis demonstrated that psbE is transcribed into a 0.3 kb mRNA, while transcription of psbF and psbL genes results in a 0.9 kb transcript. The splitting of the psbEFLJ operon into separate transcription units suggests a unique mechanism of regulation of expression of these genes in C. reinhardtii.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00298966
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  • 7
    Electronic Resource
    Electronic Resource
    Directed inactivation of the psbl gene does not affect Photosystem II in the cyanobacterium Synechocystis sp. PCC 6803 (1995)
    Springer
    Molecular genetics and genomics 249 (1995), S. 622-628 
    Details
    ISSN: 1617-4623
    Keywords: Photosynthesis ; Photosystem II ; Oxygen evolution ; Targeted mutagenesis ; Light sensitivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract PsbI is a small, integral membrane protein component of photosystem II (PSII), a pigment-protein complex in cyanobacteria, algae and higher plants. To understand the function of this protein, we have isolated the psbI gene from the unicellular cyanobacterium Synechocystis sp. PCC 6803 and determined its nucleotide sequence. Using an antibiotic-resistance cartridge to disrupt and replace the psbI gene, we have created mutants of Synechocystis 6803 that lack the PsbI protein. Analysis of these mutants revealed that absence of the PsbI protein results in a 25–30% loss of PSII activity. However, other PSII polypeptides are present in near wild-type amounts, indicating that no significant destabilization of the PSII complex has occurred. These results contrast with recently reported data indicating that PsbI-deficient mutants of the eukaryotic alga Chlamydomonas reinhardtii are highly light-sensitive and have a significantly lower (80–90%) titer of the PSII complex. In Synechocystis 6803, PsbI-deficient cells appear to be slightly more photosensitive than wild-type cells, suggesting that this protein, while not essential for PSII biogenesis or function, plays a role in the optimization of PSII activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00418031
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  • 8
    Electronic Resource
    Electronic Resource
    Struktur, Funktion, Biogenese und Evolution des Photosystems II (1999)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 29 (1999), S. 36-43 
    Details
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Das Photosystem II (PSII) ist der größte Pigment-Protein-Komplex in der Thylakoidmembran höherer Pflanzen, in eukaryotischen Algen und in prokaryotischen Cyanobakterien. Seine Funktion besteht in der Übertragung von Elektronen von Wasser auf Plastochinone, wobei Sauerstoff freigesetzt wird. Die Energie für diese Reaktion wird vom Sonnenlicht geliefert, welches über eine große Anzahl von Pigmenten (Chlorophylle, Carotinoide, Physcobiline) absorbiert wird. Nach deren Anregungen wird die Energie auf ein besonderes Chlorophyll, das P680 im Reaktionszentrum, weitergeleitet. Danach werden eine Reihe von Redoxreaktionen ausgelöst, die letztendlich zur Synthese von ATP und NADPH an der Photosynthesemembran führen. Die Sauerstoff-freisetzende (oxygene) Photosynthese scheint vor mehr als 3,8 Millionen Jahren etabliert worden zu sein, und die wesentliche Organisation und die Struktur des PSII sind während der Evolution des Pflanzenreichs weitgehend erhalten geblieben.In eukaryotischen Organismen (Pflanzen und eukaryotischen Algen) befinden sich die Gene für die PSII-Protein teilweise im Plastidengenom (Plastom) und teilweise im Kerngenom (Tabelle 1). Der Grund könnte folgender gewesen sein: Die im Zellkern vorhandenen Gene codieren entweder Komponenten, die au f der prokaryotischen Ebene noch nicht vorhanden waren (beispielsweise die luminalen 23 und 16 Kilodalton (kDa) Polypeptide), oder sie wurden vom cyanobakteriellen Genom nach der Endosymbiose in den Zellkern übertragen (beispielsweise das luminale 33 kDa Protein, siehe unten). Durch die Aufteilung der genetischen Information auf die beiden Kompartimente konnte die Symbiose stabilisiert werden, da der Eindringling nun nicht mehr unabhängig vom Wirt leben konnte. Obwohl die Mechanismen, welche die Expression der im Zellkern und in der Plastide codierten Gene steuern, sehr unterschiedlich sind und die Kopienzahlen der einzelnen Gene zwischen 1 und 10000 schwanken können, ist es erstaunlich, daß eine derartig effiziente Regulation der Expression und der Zusammenlagerung (Assemblierung) des Komplexes stattfindet.In diesemk Artikel sollen Form, Funktion, Biogenese und Evolution des PSII-Komplexesd von prokaryotischen blaugrünen Algen, Grünalgen und höheren Pflanzen verglichen werden. Weiterer Schwerpunkt ist die Lokalisation und Expression von Genen, die für Strukturkomponenten vom PSII codieren. Schließlich wird noch auf solche Komponenten eingegangen, die regulatorische Funktionen beui der Assemblierung dieses Multiproteinkomplexes besitzen.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.960290107
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