Synechococcus sp. PCC

Ito Y, Butler A (2005) Structure of Synechobactins, New Siderophores of the Marine Cyanobacterium Synechococcus sp. PCC 7002. Limnol Oceanogr 50 1918... 

Shen et al.266 inactivated the rubA gene in Synechococcus sp. PCC 7002 and could show that all three Fe-S dusters are missing. The preparation was characterized by various spectroscopic methods including several EPR techniques. The results showed that the A binding site is intact and virtually identical to that of wild type. 

In recent work Shen et al.336 inactivated a gene in Synechococcus sp. PCC 7002... 

Gardner, G. (1981). Azidoatrazine Photoaffinity label for the site of triazine herbicide action in chloroplasts. Science, 211 937-940. Gingrich, J.C., J.S. Buzby, V.L. Stirewalt, and D.A. Bryant (1988). Genetic analysis of two new mutations resulting in herbicide resistance in the cyanobacterium Synechococcus-sp pcc 7002. Photosyn. Res., 16 83-100. 

Luque, L, Contreras, A., Zabulon, G., Herrero, A., and Houmard, J. (2002). Expression of the glutamyl-tRNA synthetase gene from the cyanobacterium Synechococcus sp PCC 7942 depends on nitrogen availability and the global regulator NtcA. Mol. Microbiol. 46, 1157—1167. 

Luque, L, Flores, E., and Herrero, A. (1993). Nitrite reductase gene from Synechococcus sp. PCC 7942 Homology between cyanobacteria and higher plant nitrite reductases. Plant Mol. Biol. 21, 1202-1205. 

Suzuki, 1., Sugiyama, T., and Omata, T. (1995). Regulation of nitrite reductase activity imder CO2 limitation in the cyanobacterium Synechococcus sp. PCC 7942. Plant Physiol. 107, 791—796. 

K ssel, I D ry, G Igloi and R Maier (1990) A leucine-zipper motif in photosystem I. Plant Mol Biol 15 497-499 L Smart, PV Warren, JH Golbeck and L McIntosh (1993) Mutational analysis of the structure and biogenesis of the photosystem I reaction center in the cyanobacterium Synechococcus sp. PCC 6803. Proc Nat Acad Sci, USA 90 1132-1136... 

Fig. 7. Amino-acid sequence alignment for PsaC [FeS-A/FeS-B] in maize, bariey, wheat, rice, spinach, Synechococcus sp. PCC 7002, pea and tobacco and, for comparison purposes, Peptococcus aerogenes and Peptostreptococcus elsdenii. See text for discussion and data sources.

IR Vassiliev Y-S Jung Pi ang and JH Golbeck (1998) PsaC subunit of photosystem I is oriented with iron-sulfur dusterpB as the immediate electron donor to ferredoxin and flavodoxin. Biophys J 74 2029-2035 Y-S Jung L Yu and JH Golbeck (1995) Reconstitution of iron-sulfur center Fb results in complete restoration of NADP photoreduction in Hg-treated photosystem I complexes from Synechococcus sp PCC 6301. Photosynthesis Res 46 249-255... 

Fig. 11. (A) Model for the homologous PsaA (and PsaB) subunits of photosystem I. Helices VIII and IX and the VIII-IX interhelical loop are shown inside the dashed ellipse (B) Amino-acid composition of the loop between helices VIII and IX in PsaA and PsaB. with the four cysteine residues numbered for Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803, respectively (separated by a slash). (C) A working model for the FeS-X domain consisting of a bundle of four a-helices (VIII and IX from PsaA and PsaB), the interhelical loops and FeS-X itself ligated to the four cysteine residues. Model in (C) is adapted from Rodday, Jun and Biggins (1993) Interaction of the Ff Fg-containing subunit with the photosystem I core heterodimer. Photosynthesis Res 36 3.

Fig. 12. Amino-acid sequence of PsaC of Synechococcus sp. PCC 7002 (top row). Cysteine ligands (in boxes) for the FeS-A or FeS-B clusters are marked by A or "B", respectively. The acidic residues (aspartate and glutamate) are marked by "0. Amino-acid sequence of P. aeragrenes ferredoxin shown in second row. Panel (A) the KamlowskI model showing orientation of the PsaC subunit relative to FeS-X. Panei (B) P. aerogenes ferredoxin, as a simulator for PsaC, is aligned with the PS-I core binding site.

The effects of the unsaturation of fatty acids on membrane fluidity has also been extensively studied in two strains of cyanobacteria, Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7942 (Los and Murata, 2004). The genes for four specific acyl-lipid desaturases, designated desA, desB, desC and desD, have been cloned from Synechocystis. These desaturases introduce double bonds at the A12 (Sakamoto and Bryant, 1997), ( 3 (Sakamoto et al., 1994a), A9 (Sakamoto and Bryant, 1997 Sakamoto et al., 1994b), and A6 (Reddy et al.,... 

Trick CG and Wilhelm SW (1995) Physiological changes in coastal marine cyanobacterium Synechococcus sp. PCC 7002 exposed to low ferric ion levels. Marine Chemistry 50 207-217. 

Nishiyama Y, Hayashi H, Watanabe T et al. Photosynthedc oxygen evolution is stabilized by cytochrome C550 against heat inactivation in Synechococcus sp. PCC 7002. Plant Physiol 1994 105 1313-1319. 

Rouillon R, Tocabens M, Carpentier R. A photoelectrochemical cell for detecting pollutant-induced effects on the activity of immobilized cyanobacterium Synechococcus sp. PCC 7942. Enzyme Microb Tech 1999 25 230-235. 

Whole cells of Synechococcus sp. PCC 7942 2 Entrapment in PVA-SbQ Electrochemical measurement HgCb... 

Metabolic engineering of Synechococcus sp. PCC 7002 to produce poly-3-hydroxybutyrate and poly-3-hydroxybutyrate-co-4-hydroxybutyrate. 

The PS I complexes of both species were purified, and low-molecular mass polypeptides were isolated from each by preparative electrophoresis and subjected to amino-terminal amino acid sequencing. Partial sequences were obtained for the psaC, psaD, psaE, and putative psaF gene products from Synechococcus sp. PCC 7002 partial sequences for the psaD and psaE gene products of Nos toe sp. PCC 8009 were also determined (19). The putative psaF product of Nostoe sp. was blocked. 

The psaD gene of Nostoc sp. PCC 8009 was cloned by low-stringency heterologous hybridization using probes derived frogi the tomato psaD cDNA (20) and the Synechococcus sp. PCC 6301 psaD gene (J. Omaha and A. 

Phycobilisomes (PBsomes) constitute the light-harvesting antennae of cyanobacteria. Most of them are made up of a central three-cylinder core from which six rods radiate (1). However, exceptions have been described i) Synechococcus sp. PCC 6301 and 7942 have hemidiscoidal PBsomes, but the six rods radiate from a core made up of only two cylinders (2) ii) according to the observed ratio of rod phycobiliproteins (PB) versus core PBs, as well as to electron microscopy studies, Phormidium sp. PCC 7376 seems to have PBsomes resembling more closely the hemi-ellipsoidal tyjpt described for most of the rhodophytes (3) iii) finally, Gloeobacter violaceus, which does not have classical thylakoid membranes, harbors very peculiar rod-shaped PBsomes directly attached to the cytoplasmic membrane (4). 

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