UVBR (ultraviolet-B radiation: 280 to 315 nm)-induced DNA damage, measured as cyclobutane pyrimidine dimers (CPDs), was determined in size fractions of natural populations of bacterio- and phytoplankton collected in marine tropical waters. Mean biologically effective UVBR doses in the wind-mixed layer were calculated from DNA dosimeter data. Phytoplankton species composition in these waters was monitored using flow cytometry and pigment analyses. In terms of (divinyl-)chlorophyll a concentrations, prochlorophytes and cyanobacteria comprised the largest fraction of the phytoplankton, except in a eutrophic bay at Curacao an island located in the southern Caribbean. In terms of cell numbers and amount of DNA, small prochlorophytes and marine bacteria dominated. Small but detectable levels of UVBR-induced DNA damage were found at all locations. In general, more DNA damage was found in the small size fraction (0.2 to 1 mu m) than in the larger size fraction (1 to 10 mu m). The greatest amount of ...

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The synthesis of bacteriochlorophyll (Bchl) was inhibited in wild type strain of Rhodopseudomonas capsulata by levulinic acid (LA), δ-aminolevulinic acid of α,α′-dipyridyl. The transcription of genes for pigment-binding proteins, the synthesis and incorporation of these proteins into the membrane and the assembly of photosynthetic complexes were studied. Inhibition of Bchl synthesis did not impair formation of mRNA for pigment-binding polypeptides, but inhibited the synthesis of these proteins as well as stable incorporation into the membrane. The results let suggest, that Bchl is necessary for the stabilization of pigment-binding proteins in the membrane, and that intermediates of Bchl-synthesis affect the synthesis of these proteins. The same experiments were carried out with mutant strains blocked in Bchl synthesis. All Bchl-less mutant strains investigated here, showed transcription of photosynthetic genes at a rate which was independent of oxygen tension. The synthesis of polypeptides of

Three surface residues of plastocyanin from Prochlorothrix hollandica have been modified by site-directed mutagenesis. Changes have been made in methionine 33, located in the hydrophobic patch of the copper protein, and in arginine 86 and proline 53, both located in the eastern hydrophilic area. The reactivity toward photosystem I of single mutants M33N, P53A, P53E, R86Q, R86E, and the double mutant M33N/P14L has been studied by laser flash absorption spectroscopy. All the mutations yield increased reactivity of plastocyanin toward photosystem I as compared with wild type plastocyanin, thus indicating that in Prochlorothrix electron donation to photosystem I is not optimized. The most drastic increases in the intracomplex electron transfer rate are obtained with mutants in methionine 33, whereas replacing arginine 86 only modestly affects the plastocyanin-photosystem I equilibrium constant for complex formation. Mutations at position 53 also promote major changes in the association of ...

The Evolution of Far-Red Light Perception in Acaryochloris Marina, a Chlorophyll d-Containing Cyanobacterium Conference Paper ...

Astyanax fasciatus B23 protein: a blue visual pigment protein; expressed in the retina of fish, Astyanax fasciatus; has high homology to the goldfish blue visual pigment; do not confuse with nucleolar protein B23, a phosphoprotein; aa sequence given in first source

Mutations in the visual pigment protein rod opsin are the most common cause of autosomal dominant retinitis pigmentosa (ADRP) and the majority of these mutations lead to the misfolding of the protein. Patients with ADRP experience progressive loss of vision leading to blindness and at the moment no effective therapy is available. In this study I have developed a cellular model that can mimic the gain-of function and dominant-negative disease mechanisms in rhodopsin ADRP patients. Whereas wild-type rod opsin translocated to the plasma membrane of the cells, P23H mutant rod opsin misfolded was retained in the ER and accumulated in intracellular inclusions. Several pharmacological compounds were tested in this model. The retinoids 9-c/s-retinal and 11-c/s-retinal reduced inclusion incidence, alleviated cell death and promoted the translocation of the mutant protein to the plasma membrane in cells expressing P23H rod opsin. In cells co-expressing wild-type and P23H rod opsin these compounds restored ...

ID ACAM1_1_PE1876 STANDARD; PRT; 111 AA. AC ACAM1_1_PE1876; B0CEK1; DT 00-JAN-0000 (Rel. 1, Created) DT 00-JAN-0000 (Rel. 2, Last sequence update) DT 00-JAN-0000 (Rel. 3, Last annotation update) DE SubName: Full=Rare lipoprotein A; (ACAM1_1.PE1876). GN Name=rlpA; OrderedLocusNames=AM1_1950; OS ACARYOCHLORIS MARINA MBIC11017. OC Bacteria; Cyanobacteria; Acaryochloris. OX NCBI_TaxID=329726; RN [0] RP -.; RG -.; RL -.; CC -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE1876. CC Acaryochloris marina MBIC11017, complete genome. CC -!- ANNOTATIONS ORIGIN:B0CEK1_ACAM1 CC -!- SIMILARITY: Belongs to the rlpA family. CC -!- GENE_FAMILY: HOG000254768 [ FAMILY / ALN / TREE ] DR UniProtKB/Swiss-Prot; B0CEK1; -. DR EMBL; CP000828; ABW26967.1; -; Genomic_DNA. DR RefSeq; YP_001516281.1; NC_009925.1. DR ProteinModelPortal; B0CEK1; -. DR STRING; B0CEK1; -. DR GeneID; 5680765; -. DR GenomeReviews; CP000828_GR; AM1_1950. DR KEGG; amr:AM1_1950; -. DR OMA; NTHAMTA; -. DR ProtClustDB; CLSK2328797; -. ...

ID ACAM1_1_PE4314 STANDARD; PRT; 54 AA. AC ACAM1_1_PE4314; B0CF05; DT 00-JAN-0000 (Rel. 1, Created) DT 00-JAN-0000 (Rel. 2, Last sequence update) DT 00-JAN-0000 (Rel. 3, Last annotation update) DE RecName: Full=Sec-independent protein translocase protein tatA/E homolog DE 1; (ACAM1_1.PE4314). GN Name=tatA1; OrderedLocusNames=AM1_4425; OS ACARYOCHLORIS MARINA MBIC11017. OC Bacteria; Cyanobacteria; Acaryochloris. OX NCBI_TaxID=329726; RN [0] RP -.; RG -.; RL -.; CC -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE4314. CC Acaryochloris marina MBIC11017, complete genome. CC -!- ANNOTATIONS ORIGIN:B0CF05_ACAM1 CC -!- FUNCTION: Required for correct localization of precursor proteins CC bearing signal peptides with the twin arginine conserved motif CC S/T-R-R-X-F-L-K. This sec-independent pathway is termed TAT for CC twin-arginine translocation system. This system mainly transports CC proteins with bound cofactors that require folding prior to export CC (By similarity). CC -!- ...

p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...

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Oxygenic photosynthesis converts light-energy into chemical free energy by reducing NADP$\sp+$ to NADPH and producing ATP. Eukaryotic plants and algae as well as prokaryotic cyanobacteria and prochlorophytes have a similar photosynthetic apparatus. The light-driven reactions take place in the thylakoid membranes and three major membrane-intrinsic protein complexes carry out photosynthetic electron transfer, photosystem II, the cytochrome bf complex and photosystem I. To elucidate photosynthetic electron transport in oxygenic photosynthesis site-directed mutagenesis and biophysical techniques were employed in cyanobacteria which have the advantage over plants that they are easily genetically manipulated. This work focused on electron transfer linking the cytochrome bf complex and photosystem I, characterization of the plastoquinol oxidation site of the cytochrome bf complex and electron transfer within the PsaC polypeptide of the photosystem I complex. Major findings include (1) in vivo electron ...

When deprived of essential nutrients, the non-diazotrophic cyanobacterium Synechococcus sp. strain PCC 7942 undergoes a proteolytic degradation of the phycobiliproteins, its major light-harvesting pigments. This process is known as chlorosis. This paper presents evidence that the degradation of phycobiliproteins is part of an acclimation process in which growing cells differentiate into non-pigmented cells able to endure long periods of starvation. The time course of degradation processes differs for various photosynthetic pigments, for photosystem I and photosystem II activities and is strongly influenced by the illumination and by the experimental conditions of nutrient deprivation. Under standard experimental conditions of combined nitrogen deprivation, three phases of the differentiation process can be defined. The first phase corresponds to the well-known phycobiliprotein degradation, in phase 2 the cells lose chlorophyll a prior to entering phase 3, the fully differentiated state, in which the

General Information: Acaryochloris marina MBIC11017 was isolated from algae from the coast of the Palau Islands in the western Pacific. Marine cyanobacterium. Acaryochloris marina was first isolated as an epiphyte of algae. M. marina been isolated from a variety of habitats and locations, usually associated with algae but also as free-living organisms. This cyanobacterium produces an atypical photosynthetic pigment, chlorophyll d, as the major reactive agent. The oxygenic photosynthesis based on this pigment may have evolved as an acclimatization to far-red light environments, or an as intermediate between the red-absorbing oxygenic and the far-red-absorbing anoxygenic photosynthesis that uses bacteriochlorophylls. Because of the unusual ratio of chlorophyll a to chlorophyll d in this organism, it has been used as a model to study the spectrographic characteristics of the two pigments. ...

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Understanding of electronic energy transition (EET) mechanisms from the light-harvesting unit to the reaction centre in a natural system has been limited by; (a) the use of conventional transient time-resolved spectroscopy at room temperature, which result in high signal-to-noise ratio; and (b) examining extracts instead of intact light-harvesting units. Here, we report previously unknown differences and new insight in EET of two cyanobacteria species, Acaryochloris marina and Thermosynechoccocus vulvanus, which have been found only after using Uv-vis, hole-burning and fluorescence spectroscopy at ultra-low temperature and examining their intact light-harvesting unit, phycobilisomes (PBS ...