The Diversity of Retinylidene Proteins in Microorganisma

微生物中视黄基蛋白的多样性

• 批准号: 06672139
• 负责人: TAKAHASHI Tetsuo
• 金额: $ 1.41万
• 依托单位: Japan Advanced Institute of Science and Technology
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (C)
• 财政年份: 1994
• 资助国家: 日本
• 起止时间: 1994 至 1995
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-06672139/
• 关键词: Phototaxis; Rhodopsin; Retinal; Chlamydomonas; Halobacteria; Archaebacteria; Behavior; Chemotaxis; Ectothiorhodospra halophila; Halobacterium halobium; Halobacterium salinarium; ISH; sensory vhodopsin; phoborhodopsin; H.halobium; phototaxis

The absorption spectrum of phoborhodopsin (PR) of Halobacterium salinarium (H.salinarium) exhibits unique features : (1) The absorption maximum is nearly 100-nm blue shifted from those of other bacterial rhodopsins. (2) It shows vibrational fine structure at ambient temperatures. Our recent results are : .1.13-demethyl retinal analog reconstitutes inverted photophobic responses in PR,while this analog confers no photochemical (of course no photobehavioral) activity to SR-I.2. Conformation at C6-C7 bond of the chromophore has been confirmed to be s-trans in PR,whereas the chromophore binding site in PR is not so restricted like other archaebacterial rhodopsins. This has been the conclusion of an analog-reconstitution study using the both trans and cis retinal analogs in which C6-C7 conformation was locked with either a 5-membered or a 7-membered ring. Interestingly, PR analog pigment has been reconstituted from 6-s-cis locked (with 7-membered ring) retinal, which has a C5=C6-C7=C8 structure close to the native retinal at the chromophore binding site of visual rhodopsin. However, this PR analog showed no vibrational fine structure.3. The primary sequence of PR in H.salinarium has been obtained quite recently, showing close homology to the related pigments of Natronobacterium pharaonis and Haloarcula vallismortis as well as bacteriorhodopsin (see also Zhang et al.Proc.Natl.Acad.Sci.93,8230-8235,1996) This and the above results confirmed that PR is a genuine member of the family of archaebacterial rhodopsins, leaving the unsolved problem of possible phylogenic relationship between archaebacterial rhodopsins and animal visual pigments.

盐生盐杆菌（Halobacteriumsalinarium，H.salinarium）的视紫红质（phoborhodopsin，PR）具有独特的吸收光谱：（1）其最大吸收波长比其它细菌的视紫红质蓝移近100 nm; (2)它在室温下显示出振动精细结构。我们最近的结果是：1.13-去甲基视黄酸类似物在PR中重建了反向的憎水反应，而这种类似物不赋予SR-I光化学（当然没有光行为）活性。PR的发色团C6-C7键构象被证实是s-反式的，而PR的发色团结合位点不像其他古细菌视紫红质那样受到如此限制。这是使用反式和顺式视黄醇类似物的类似物重建研究的结论，其中C6-C7构象被5元或7元环锁定。有趣的是，PR类似物色素已经从6-顺式锁定（具有7元环）的视黄醛重构，其具有在视紫红质的发色团结合位点处接近天然的视黄醛的C5=C6-C7=C8结构。然而，这种PR类似物没有显示出振动精细结构.盐生盐杆菌PR基因的一级序列与盐生盐杆菌（Natronobacterium pharaonis）和盐生盐菌（Haloarcula vallismortis）的相关色素以及细菌视紫红质（bacteriorhodopsin）的同源性较高（也参见Zhang等，Proc.Natl.Acad.Sci.93，8230 - 8235，1996）这一结果和上述结果证实PR是古细菌视紫红质家族的真正成员，留下了古细菌视紫红质和动物视色素之间可能的遗传关系的未解决的问题。

项目成果

Erata, M., Kubota, M., Takahashi, T., Inoue, I.and Watanabe, M.: "Ultrastructure and phototactic action spectra of two genera of cryptophyte flagellate algae, Cryptomonas and Chroomonas" Protoplasma. 188. 258-266 (1995)

Erata, M.、Kubota, M.、Takahashi, T.、Inoue, I. 和 Watanabe, M.：“隐藻鞭毛藻两个属的超微结构和趋光作用光谱，隐单胞菌属和色单胞菌属”原生质体。

Mayumi Erata: "Ultrastracture and Phototactic Action Spectra of Two Genera of Cryptophyte Flagellate Algae,Cryptomonas and Chroomonas" Protoplasma.

Mayumi Erata：“隐藻鞭毛藻、隐单胞菌和色单胞菌两个属的超结构和趋光作用光谱”原生质体。

Erata,M.,Kubota,M.,Takahashi,T.,Inoue,I,Watanabe,M.: "Ultrastracture and phototactic action spectra of two genera of cryptophyte flagellate algre,Cryptomonas and Chroomonas." Protoplasma. 188. 258-266 (1995)

Erata，M.，Kubota，M.，Takahashi，T.，Inoue，I，Watanabe，M.：“隐藻鞭毛虫两个属，隐单胞菌属和色单胞菌属的超结构和趋光作用光谱。”

Mayumi Evata: "Ultrastructure and phototartic action spectra of two genera of cryptophyto flagelate algae,Cryptomonas and Chroomonas" Protoplasma. 188. 258-266 (1995)

Mayumi Evata：“隐藻鞭毛藻两个属的超微结构和光致反应光谱，隐单胞菌和色单胞菌”原生质体。