ロドスピリラム・ラブラム、ロドスピリルム・ラブラム
[show details]
- 関
- R. rubrum
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/08/21 16:21:49」(JST)
[Wiki en表示]
| Rhodospirillum rubrum |
| Scientific classification |
| Kingdom: |
Bacteria |
| Phylum: |
Proteobacteria |
| Class: |
Alphaproteobacteria |
| Order: |
Rhodospirillales |
| Family: |
Rhodospirillaceae |
| Genus: |
Rhodospirillum |
| Species: |
R. rubrum |
| Binomial name |
Rhodospirillum rubrum
|
Rhodospirillum rubrum (R. rubrum) is a Gram-negative, purple-coloured Proteobacterium, with a size of 800 to 1000 nanometers.
It is a facultative anaerobe, it can therefore use alcoholic fermentation under low oxygen conditions or use aerobic respiration in aerobic conditions. Under aerobic growth photosynthesis is genetically suppressed and R. rubrum is then colorless. After the exhaustion of oxygen, R. rubrum immediately starts the production of photosynthesis apparatus including membrane proteins, bacteriochlorophylls and carotenoids, i.e. the bacterium becomes photosynthesis active. The repression mechanism for the photosynthesis is poorly understood. The photosynthesis of R. rubrum differs from that of plants as it possesses not chlorophyll a, but bacteriochlorophylls. While bacteriochlorophyll an absorbs light having a maximum wavelength of 800 to 925 nm, chlorophyll absorbs light having a maximum wavelength of 660 to 680 nm. R. rubrum is a spiral-shaped bacterium (spirillum, plural form: spirilla).
R. rubrum is also a nitrogen fixing bacterium, i.e., it can express and regulate nitrogenase, a protein complex that can catalyse the conversion of atmospheric dinitrogen into ammonia. Due to this important property, R. rubrum has been the test subject of many different groups, so as to understand the complex regulatory schemes required for this reaction to occur (,[1][2][3][4] among others). It was in R. rubrum that, for the first time, post-translational regulation of nitrogenase was demonstrated. Nitrogenase is modified by an ADP-ribosylation in the arginine residue 101 (Arg101)[5] in response to the so-called "switch-off" effectors - glutamine or ammonia - and darkness.[6]
R. rubrum has several potential uses in biotechnology:
- Quantitative accumulation of PHB (poly-hydroxy-butric-acid) precursors in the cell for the production of biological plastic
- Production of biological hydrogen fuel
- Model system for studying the conversion from light energy to chemical energy and regulatory pathways of the nitrogen fixation system.
References[edit source | edit]
- ^ Teixeira PF, Jonsson A, Frank M, Wang H, Nordlund S (2008). "Interaction of the signal transduction protein GlnJ with the cellular targets AmtB1, GlnE and GlnD in Rhodospirillum rubrum: dependence on manganese, 2-oxoglutarate and the ADP/ATP ratio". Microbiology 154 (Pt8): 2336–47. doi:10.1099/mic.0.2008/017533-0. PMID 18667566.
- ^ Selao TT, Nordlund S, Norén A (2008). "Comparative proteomic studies in Rhodospirillum rubrum grown under different nitrogen conditions". J Proteome Res 7 (8): 3267–75. doi:10.1021/pr700771u. PMID 18570453.
- ^ Wolfe DM, Zhang Y, and Roberts GP (2007). "Specificity and Regulation of Interaction between the PII and AmtB1 Proteins in Rhodospirillum rubrum". J Bacteriol 189 (19): 6861–6869. doi:10.1128/JB.00759-07. PMC 2045211. PMID 17644595.
- ^ Jonsson A, Teixeira PF, Nordlund S (2007). "The activity of adenylyltransferase in Rhodospirillum rubrum is only affected by alpha-ketoglutarate and unmodified PII proteins, but not by glutamine, in vitro". FEBS J 274 (10): 2449–60. doi:10.1111/j.1742-4658.2007.05778.x. PMID 17419734.
- ^ Pope MR, Murrell SA, Ludden PW (1985). "Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue". Proc Natl Acad Sci U S A 82 (10): 3173–7. doi:10.1073/pnas.82.10.3173. PMC 397737. PMID 3923473.
- ^ Neilson AH, Nordlund S (1975). "Regulation of nitrogenase synthesis in intact cells of Rhodospirillum rubrum: inactivation of nitrogen fixation by ammonia, L-glutamine and L-asparagine". J Gen Microbiol 91 (1): 53–62. PMID 811763.
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Site-specific genome integration in alphaproteobacteria mediated by TG1 integrase.
- Morita K, Morimura K, Fusada N, Komatsu M, Ikeda H, Hirano N, Takahashi H.SourceDepartment of Applied Biological Science, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-shi, Kanagawa, 252-0880, Japan.
- Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2011 Sep 2. [Epub ahead of print]
- The serine-type phage integrase is an enzyme that catalyzes site-specific recombination between two attachment sites of phage and host bacterial genomes (attP and attB, respectively) having relatively short but distinct sequences without host auxiliary factor(s). Previously, we have established in v
- PMID 21887508
- The poor growth of Rhodospirillum rubrum mutants lacking RubisCO is due to the accumulation of ribulose-1,5-bisphosphate.
- Wang D, Zhang Y, Pohlmann EL, Li J, Roberts GP.SourceDepartment of Microbiology and Immunology, China Agricultural University, Beijing 100193, People’s Republic of China.
- Journal of bacteriology.J Bacteriol.2011 Jul;193(13):3293-303. Epub 2011 Apr 29.
- Ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) catalyzes the first step of CO(2) fixation in the Calvin-Benson-Bassham (CBB) cycle. Besides its function in fixing CO(2) to support photoautotrophic growth, the CBB cycle is also important under photoheterotrophic growth conditions in purple
- PMID 21531802
Japanese Journal
- 23aPS-34 フェムト秒時間分解吸収分光を用いた紅色光合成細菌Rhodospirillum rubrum S1の超高速エネルギー移動の観測(23aPS 領域5ポスターセッション(光電子分光・光誘起相転移等),領域5(光物性))
- 丸田 聡,堀部 智子,小澄 大輔,藤井 律子,杉崎 満,橋本 秀樹
- 日本物理学会講演概要集 65(1-4), 804, 2010-03-01
- NAID 110007656790
- ガスセンサーＣｏｏＡとＦｉｘＬとＤｏｓに関する最近の研究
- 山下 沢
- 薬学雑誌 130(9), 1181-1187, 2010
- … CooA is a CO-sensing transcriptional activator derived from the photosynthetic bacterium Rhodospirillum rubrum. …
- NAID 130000342378
- ポリエステルの微生物分解 : Ralstonia metalliduransにおけるPHB結合蛋白質の役割の検討(2005年度神奈川大学総合理学研究所協同研究助成論文)
- 齊藤 光實
- Science Journal of Kanagawa University 17, 81-82, 2006-05-25
- … Although GAP2 accelerated the degradation of the PHB inclusion body in a similar manner to Apd from Rhodospirillum rubrum, the physiological role of GAP2 was not clear. …
- NAID 110004997361
Related Links
- R. rubrum has not been found to infect humans or animals. Current Research Radiation resistance Rhodospirillum rubrum has recently provided insight into radiation resistance. Felice Mastroleo et al, in Insight into the radiotolerance ...
- Rhodospirillum is a genus of photosynthetic bacteria of the family Rhodospirillaceae. Their cells are generally spiral-shaped, polarly flagellated and contain vesicular, lamellar of stacked photosynthetic membranes ...
Related Pictures
★リンクテーブル★
[★]
- ラ
- Rhodospirillum rubrum、R. rubrum
- 関
- ロドスピリルム・ラブラム
[★]
- ラ
- Rhodospirillum rubrum
- 関
- ロドスピリラム・ラブラム
[★]
- 関
- Rhodospirillum rubrum
[★]
ロドスピリラム、ロドスピリルム、ドスピリラム属、ロドスピリルム属、Rhodospirillum属
- 関
- purple nonsulfur bacteria、Rhodospirillaceae、Rhodospirillales