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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/14 03:25:54」(JST)
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English Journal
- Monomeric RC-LH1 core complexes retard LH2 assembly and intracytoplasmic membrane formation in PufX-minus mutants of Rhodobacter sphaeroides.
- Adams PG, Mothersole DJ, Ng IW, Olsen JD, Hunter CN.AbstractIn the model photosynthetic bacterium Rhodobacter sphaeroides domains of light-harvesting 2 (LH2) complexes surround and interconnect dimeric reaction centre-light-harvesting 1-PufX (RC-LH1-PufX) 'core' complexes, forming extensive networks for energy transfer and trapping. These complexes are housed in spherical intracytoplasmic membranes (ICMs), which are assembled in a stepwise process where biosynthesis of core complexes tends to dominate the early stages of membrane invagination. The kinetics of LH2 assembly were measured in PufX mutants that assemble monomeric core complexes, as a consequence of either a twelve-residue N-terminal truncation of PufX (PufXΔ12) or the complete removal of PufX (PufX(-)). Lower rates of LH2 assembly and retarded maturation of membrane invagination were observed for the larger and less curved ICM from the PufX(-) mutant, consistent with the proposition that local membrane curvature, initiated by arrays of bent RC-LH1-PufX dimers, creates a favourable environment for stable assembly of LH2 complexes. Transmission electron microscopy and high-resolution atomic force microscopy were used to examine ICM morphology and membrane protein organisation in these mutants. Some partitioning of core and LH2 complexes was observed in PufX(-) membranes, resulting in locally ordered clusters of monomeric RC-LH1 complexes. The distribution of core and LH2 complexes in the three types of membrane examined is consistent with previous models of membrane curvature and domain formation (Frese et al., 2008), which demonstrated that a combination of crowding and asymmetries in sizes and shapes of membrane protein complexes drives membrane organisation.
- Biochimica et biophysica acta.Biochim Biophys Acta.2011 Sep;1807(9):1044-55. Epub 2011 Jun 2.
- In the model photosynthetic bacterium Rhodobacter sphaeroides domains of light-harvesting 2 (LH2) complexes surround and interconnect dimeric reaction centre-light-harvesting 1-PufX (RC-LH1-PufX) 'core' complexes, forming extensive networks for energy transfer and trapping. These complexes are house
- PMID 21663730
- Carotenoids are essential for normal levels of dimerisation of the RC-LH1-PufX core complex of Rhodobacter sphaeroides: Characterisation of R-26 as a crtB (phytoene synthase) mutant.
- Ng IW, Adams PG, Mothersole DJ, Vasilev C, Martin EC, Lang HP, Tucker JD, Neil Hunter C.AbstractCarotenoids play important roles in photosynthesis where they are involved in light-harvesting, in photo-protection and in the assembly and structural stability of light-harvesting and reaction centre complexes. In order to examine the effects of carotenoids on the oligomeric state of the reaction centre-light-harvesting 1 -PufX (RC-LH1-PufX) core complex of Rhodobacter sphaeroides two carotenoid-less mutants, TC70 and R-26, were studied. Detergent fractionation showed that in the absence of carotenoids LH2 complexes do not assemble, as expected, but also that core complexes are predominantly found as monomers, although levels of the PufX polypeptide appeared to be unaffected. Analysis of R-26 membranes by electron microscopy and atomic force microscopy reveals arrays of hexagonally packed monomeric RC-LH1-PufX complexes. Transfer of the crtB gene encoding phytoene synthase to TC70 and R-26 restores the normal synthesis of carotenoids demonstrating that the R-26 mutant of Rba. sphaeroides harbours a mutation in crtB, among its other defects. The transconjugant TC70 and R-26 strains containing crtB had regained their ability to assemble wild-type levels of dimeric RC-LH1-PufX core complexes and normal energy transfer pathways were restored, demonstrating that carotenoids are essential for the normal assembly and function of both the LH2 and RC-LH1-PufX complexes in this bacterial photosystem.
- Biochimica et biophysica acta.Biochim Biophys Acta.2011 Sep;1807(9):1056-63. Epub 2011 May 30.
- Carotenoids play important roles in photosynthesis where they are involved in light-harvesting, in photo-protection and in the assembly and structural stability of light-harvesting and reaction centre complexes. In order to examine the effects of carotenoids on the oligomeric state of the reaction c
- PMID 21651888
Japanese Journal
- 3P-2052 Rhodobacter sphaeroides RVのadh挿入による水素生産に関する研究(5c バイオマス,資源,エネルギー工学,一般演題,環境バイオテクノロジー,伝統の技と先端科学技術の融合)
- 宇佐美 翔太,斉田 丞,小林 淳平,小森谷 友絵,淺田 泰男,神野 英毅
- 日本生物工学会大会講演要旨集 平成22年度, 156, 2010-09-25
- NAID 110008084940
- 光合成細菌変異株を用いたレブリン酸濃度,pHの最適化,および酸化還元電位の制御による5-アミノレブリン酸の大量生産
- 田中 享,西川 誠司,渡辺 圭太郎,田中 徹,佐々木 健
- 生物工学会誌 : seibutsu-kogaku kaishi 88(9), 455-462, 2010-09-25
- すでに得ている光合成細菌変異株R.spharoides CR-720株は,N-メチル-N'-ニトロ-N-ニトロソグアニジンによる変異を逐次行い取得した変異株であり,光照射せずに従来の変異株に対して5-アミノレブリン酸(ALA)を高蓄積する.本菌株は前駆体として50mMグルコース,60mMグリシン,ALA脱水酵素阻害剤として5mMレブリン酸および10gl^<-1>酵母エキス存在下,2l発 …
- NAID 110007730754
Related Links
- Description and significance Rhodobacter sphaeroides is a rod-shaped, gram-negative, purple non-sulfur photoheterotrophic bacterium belonging to the α-3 subclass of Proteobacteria. Like other species of Rhodobacter, R. sphaeroides ...
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★リンクテーブル★
| リンク元 | 「Rhodobacter spheroides」「ロドバクター・スフェロイデス」「Rhodopseudomonas sphaeroides」「R. sphaeroides」 |
| 関連記事 | 「Rhodobacter」「sphaeroides」 |
「Rhodobacter spheroides」
;関:Rhodobacter sphaeroides
「ロドバクター・スフェロイデス」
「Rhodopseudomonas sphaeroides」
「R. sphaeroides」
「Rhodobacter」
紅色細菌、ロドバクター、ドバクター属、Rhodobacter属
「sphaeroides」