English Journal

Ferredoxin:thioredoxin reductase (FTR) links the regulation of oxygenic photosynthesis to deeply rooted bacteria.

Balsera M1, Uberegui E, Susanti D, Schmitz RA, Mukhopadhyay B, Schürmann P, Buchanan BB.Author information 1Instituto de Recursos Naturales y Agrobiología de Salamanca, Salamanca, Spain. monica.balsera@irnasa.csic.esAbstractUncovered in studies on photosynthesis 35 years ago, redox regulation has been extended to all types of living cells. We understand a great deal about the occurrence, function, and mechanism of action of this mode of regulation, but we know little about its origin and its evolution. To help fill this gap, we have taken advantage of available genome sequences that make it possible to trace the phylogenetic roots of members of the system that was originally described for chloroplasts-ferredoxin, ferredoxin:thioredoxin reductase (FTR), and thioredoxin as well as target enzymes. The results suggest that: (1) the catalytic subunit, FTRc, originated in deeply rooted microaerophilic, chemoautotrophic bacteria where it appears to function in regulating CO(2) fixation by the reverse citric acid cycle; (2) FTRc was incorporated into oxygenic photosynthetic organisms without significant structural change except for addition of a variable subunit (FTRv) seemingly to protect the Fe-S cluster against oxygen; (3) new Trxs and target enzymes were systematically added as evolution proceeded from bacteria through the different types of oxygenic photosynthetic organisms; (4) an oxygenic type of regulation preceded classical light-dark regulation in the regulation of enzymes of CO(2) fixation by the Calvin-Benson cycle; (5) FTR is not universally present in oxygenic photosynthetic organisms, and in certain early representatives is seemingly functionally replaced by NADP-thioredoxin reductase; and (6) FTRc underwent structural diversification to meet the ecological needs of a variety of bacteria and archaea.
Planta.Planta.2013 Feb;237(2):619-35. doi: 10.1007/s00425-012-1803-y. Epub 2012 Dec 6.
Uncovered in studies on photosynthesis 35 years ago, redox regulation has been extended to all types of living cells. We understand a great deal about the occurrence, function, and mechanism of action of this mode of regulation, but we know little about its origin and its evolution. To help fill th
PMID 23223880

Identification of a novel small RNA modulating Francisella tularensis pathogenicity.

Postic G1, Dubail I, Frapy E, Dupuis M, Dieppedale J, Charbit A, Meibom KL.Author information 1INSERM U1002, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Médecine, Paris, France.AbstractFrancisella tularensis is a highly virulent bacterium responsible for the zoonotic disease tularemia. It is a facultative intracellular pathogen that replicates in the cytoplasm of host cells, particularly in macrophages. Here we show that F. tularensis live vaccine strain (LVS) expresses a novel small RNA (sRNA), which modulates the virulence capacities of the bacterium. When this sRNA, designated FtrC (for Francisella tularensis RNA C), is expressed at high levels, F. tularensis replicates in macrophages less efficiently than the wild-type parent strain. Similarly, high expression of FtrC reduces the number of viable bacteria recovered from the spleen and liver of infected mice. Our data demonstrate that expression of gene FTL_1293 is regulated by FtrC. Furthermore, we show by in vitro gel shift assays that FtrC interacts specifically with FTL_1293 mRNA and that this happens independently of the RNA chaperone Hfq. Remarkably, FtrC interacts only with full-length FTL_1293 mRNA. These results, combined with a bioinformatic analysis, indicate that FtrC interacts with the central region of the mRNA and hence does not act by sterically hindering access of the ribosome to the mRNA. We further show that gene FTL_1293 is not required for F. tularensis virulence in vitro or in vivo, which indicates that another unidentified FtrC target modulates the virulence capacity of the bacterium.
PloS one.PLoS One.2012;7(7):e41999. doi: 10.1371/journal.pone.0041999. Epub 2012 Jul 25.
Francisella tularensis is a highly virulent bacterium responsible for the zoonotic disease tularemia. It is a facultative intracellular pathogen that replicates in the cytoplasm of host cells, particularly in macrophages. Here we show that F. tularensis live vaccine strain (LVS) expresses a novel sm
PMID 22848684

Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC 6803 thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y) thioredoxins.

Pérez-Pérez ME1, Martín-Figueroa E, Florencio FJ.Author information 1Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, Avda Américo Vespucio 49, 41092-Sevilla, Spain.AbstractThe expression of the genes encoding the ferredoxin-thioredoxin system including the ferredoxin-thioredoxin reductase (FTR) genes ftrC and ftrV and the four different thioredoxin genes trxA (m-type; slr0623), trxB (x-type; slr1139), trxC (sll1057) and trxQ (y-type; slr0233) of the cyanobacterium Synechocystis sp. PCC 6803 has been studied according to changes in the photosynthetic conditions. Experiments of light-dark transition indicate that the expression of all these genes except trxQ decreases in the dark in the absence of glucose in the growth medium. The use of two electron transport inhibitors, 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB), reveals a differential effect on thioredoxin genes expression being trxC and trxQ almost unaffected, whereas trxA, trxB, and the ftr genes are down-regulated. In the presence of glucose, DCMU does not affect gene expression but DBMIB still does. Analysis of the single TrxB or TrxQ and the double TrxB TrxQ Synechocystis mutant strains reveal different functions for each of these thioredoxins under different growth conditions. Finally, a Synechocystis strain was generated containing a mutated version of TrxB (TrxBC34S), which was used to identify the potential in-vivo targets of this thioredoxin by a proteomic analysis.
Molecular plant.Mol Plant.2009 Mar;2(2):270-83. doi: 10.1093/mp/ssn070. Epub 2008 Nov 17.
The expression of the genes encoding the ferredoxin-thioredoxin system including the ferredoxin-thioredoxin reductase (FTR) genes ftrC and ftrV and the four different thioredoxin genes trxA (m-type; slr0623), trxB (x-type; slr1139), trxC (sll1057) and trxQ (y-type; slr0233) of the cyanobacterium Syn
PMID 19825613

Japanese Journal

抗Ｅ抗体および抗Ｄｉ｀ｂ´抗体により遅発性溶血性輸血副作用（ＤＨＴＲ）を来たした１症例

松本愼二,大川真莉子,角田麻衣,原田佑子,小島亜希,玉栄建次,棚沢敬志,平山美津江,正田絵里子,池淵研二
日本輸血細胞治療学会誌 56(4), 484-488, 2010
… ロビンの著減やLDHの上昇等が見られた．東京都赤十字血液センターにおいて精査され，輸血後患者血清中に抗E抗体と抗Dib抗体が同定された．その後E-Di（b-）で交差適合試験が適合であった解凍赤血球濃厚液（FTRC）が輸血され，輸血副作用は無く良好なHbの回復が得られた．今回の経験から，高頻度抗原に対する抗体を保有する症例では，適合血の確保に時間を要することがあるため，輸血適応の確認と不適合輸血に伴 …
NAID 130004542620

連続血球洗浄装置ACP215を用いて赤血球保存液を加えたFTRCの有効期間延長に関する検討

田村暁,秋野光明,佐藤雅子,本間稚広,山本定光,加藤俊明,池田久實
日本輸血細胞治療学会誌 = Japanese journal of transfusion and cell therapy 55(4), 508-515, 2009-09-30
NAID 10025629049

連続血球洗浄装置ACP215を用いて赤血球保存液を加えたFTRCの有効期間延長に関する検討

田村暁
日本輸血細胞治療学会誌 55, 508-515, 2009
NAID 50007261523

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