Auxiliary factors for chlorophyll biosynthesis and their potential contribution to the assembly of chlorophyll into chlorophyll-binding proteins
Auxiliary factors for chlorophyll biosynthesis and their potential contribution to the assembly of chlorophyll into chlorophyll-binding proteins
批准号:
254831670
负责人:
Professor Dr. Bernhard Grimm
金额:
$0.0万
依托单位国家:
德国
项目类别:
Research Units
财政年份:
2014
资助国家:
德国
项目状态:
已结题
起止时间:
2013-12-31 至 2021-12-31
中文摘要
叶绿素的生物合成为光合自养生物的光合作用提供了必需的色素。虽然几乎所有的酶促步骤已被阐明,时空组织的途径,以及其功能耦合到组装成光合蛋白的叶绿素仍然是悬而未决的问题。继续,该子项目的目标是:(1)深入阐明LIL 3的功能和结构作用(光捕获样蛋白3)和皮特同源质体定位的tetratricopeptide-repeat蛋白(cpTPRs)用于组织叶绿素生物合成的后期步骤,以及(ii)对叶绿素生物合成或随后与叶绿素组装的联系所需的其他辅助因子的功能作用的研究,结合蛋白,如OHP(单螺旋蛋白)、YCF 54(假设的叶绿体开放阅读框54)和CPL(POR 1(CPP 1)样蛋白的伴侣样蛋白)。它们的相互作用伙伴旨在通过先进的生物化学方法,如蛋白质亲和色谱和质谱法,或荧光和电子显微镜(部分与研究单位的合作伙伴合作),在野生型和突变植物中进行新的鉴定或确认。因此,这些生理和生化分析有助于研究单位的中心目标,以验证组装因子所需的逐步组装的光合活性蛋白质复合物在类囊体膜。
英文摘要
Chlorophyll biosynthesis provides the essential pigments for photosynthesis in photoautotrophic organisms. While almost all enzymatic steps of have been elucidated, the spatio-temporal organization of the pathway as well as its functional coupling to the assembly of chlorophyll into photosynthetic proteins are still open questions. In continuation, the objective of this subproject is (i) the in-depth elucidation of the functional and structural roles of LIL3 (light-harvesting-like protein 3) and Pitt-homologous plastid-localized tetratricopeptide-repeat proteins (cpTPRs) for the organization of the late steps of chlorophyll biosynthesis and (ii) the examination of the functional roles of additional auxiliary factors which are required either for chlorophyll biosynthesis or the subsequent link to the assembly of chlorophyll-binding proteins, such as OHP (one-helix-protein), YCF54 (hypothetical chloroplast open reading frame 54) and CPL (Chaperone-like protein of POR1 (CPP1)-like protein). Their interaction partners are aimed to be newly identified or confirmed in wild-type and mutant plants by means of advanced biochemical methods, such as protein affinity chromatography and mass spectrometry, or fluorescence and electron microscopy (in part in cooperation with partners of the Research Unit). Thereby, these physiological and biochemical analyses contribute to the central objectives of the Research Unit to validate assembly factors required for the stepwise assembly of photosynthetically active protein complexes in thylakoid membranes.
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