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首页> 外文期刊>Biochemistry >Modulation of Molecular Interactions and Function by Rhodopsin Palmitylation
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Modulation of Molecular Interactions and Function by Rhodopsin Palmitylation

机译：视紫红质棕榈酸酯化对分子相互作用和功能的调节。

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Rhodopsin is palmitylated at two cysteine residues in its carboxyl terminal region.We have lookednat the effects of palmitylation on the molecular interactions formed by rhodopsin using single-molecule forcenspectroscopy and the function of rhodopsin using both in vitro and in vivo approaches. A knockin mousenmodel expressing palmitate-deficient rhodopsin was used for live animal in vivo studies and to obtain nativentissue samples for in vitro assays. We specifically looked at the effects of palmitylation on the chromophore-nbinding pocket, interactions of rhodopsin with transducin, andmolecular interactions stabilizing the receptornstructure. The structure of rhodopsin is largely unperturbed by the absence of palmitate linkage. The bindingnpocket for the chromophore 11-cis-retinal is minimally altered as palmitate-deficient rhodopsin exhibited thensame absorbance spectrum as wild-type rhodopsin. Similarly, the rate of release of all-trans-retinal after lightnactivation was the same both in the presence and absence of palmitylation. Significant differences werenobserved in the rate of transducin activation by rhodopsin and in the force required to unfold the last stablenstructural segment in rhodopsin at its carboxyl terminal end. A 1.3-fold reduction in the rate of transducinnactivation by rhodopsin was observed in the absence of palmitylation. Single-molecule force spectroscopynrevealed a 2.1-fold reduction in the normalized force required to unfold the carboxyl terminal end ofnrhodopsin. The absence of palmitylation in rhodopsin therefore destabilizes the molecular interactionsnformed in the carboxyl terminal end of the receptor, which appears to hinder the activation of transducin bynlight-activated rhodopsin
机译：视紫红质在其羧基末端区域的两个半胱氨酸残基处被棕榈酸酯化。我们已经通过单分子力谱法研究了棕榈酸酯化对视紫红质形成的分子相互作用的影响以及使用了体内和体外方法的视紫红质的功能。表达缺失棕榈酸酯的视紫红质的敲入小鼠模型用于活体动物体内研究，并获得用于体外测定的天然组织样品。我们专门研究了棕榈酸酯化对生色团结合袋，视紫红质与转导蛋白的相互作用以及稳定受体结构的分子相互作用的影响。视紫红质的结构在很大程度上不受棕榈酸酯键的干扰。发色团11-顺-视网膜的结合口袋被最小程度地改变，因为缺乏棕榈酸酯的视紫红质表现出与野生型视紫红质相同的吸收光谱。类似地，在存在和不存在棕榈酸酯化的情况下，光激活后全反式视网膜的释放速率相同。在视紫红质激活的转导蛋白的速率以及在视紫红质的羧基末端展开最后一个稳定结构区段所需的力方面没有观察到显着差异。在没有棕榈酸酯化的情况下，视紫红质的转导激活率降低了1.3倍。单分子力谱分析揭示了展开视紫红质羧基末端所需的归一化力降低了2.1倍。因此，视紫红质中没有棕榈酸化作用会破坏在受体羧基末端形成的分子相互作用的稳定性，这似乎阻碍了光激活视紫红质对转导蛋白的激活。

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  • 来源
    《Biochemistry》 |2009年第20期|p.4294-4304|共11页
  • 作者

    Paul S.-H. Park K. Tanuj Sapra Beata Jastrzebska Tadao Maeda Akiko Maeda Wojciech Pulawski Masahiro Kono Janis Lem Rosalie K. Crouch Slawomir Filipek Daniel J. Mller and Krzysztof Palczewski;

  • 作者单位

    ‡Department of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, Ohio 44106,§Department ofPharmacology, Case Western Reserve University, Cleveland, Ohio 44106,) Biotechnology Center, University of Technology, 01307Dresden, Germany,^Department of Ophthalmology, Program in Genetics, Program in Neuroscience,Molecular Cardiology ResearchInstitute, TuftsMedical Center, Boston,Massachusetts 02111,#Department ofOphthalmology,MedicalUniversity of South Carolina,Charleston, South Carolina 29425,zInternational Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland, and &Facultyof Chemistry, University of Warsaw, 02-093, Warsaw, Poland0 Current address: Chemistry Research Laboratory,12 Mansfield Road, OX1 3TA Oxford, UK;

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