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Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly

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Science China(Life Sciences) 2011年第2期54卷 101-111页

作者： FENG Wei PAN LiFeng ZHANG MingJie Division of Life Science Molecular Neuroscience Center State Key Laboratory of Molecular Neuroscience Hong Kong University of Science and Technology Clear Water Bay Kowloon Hong Kong China National Laboratory of Biomacromolecules Institute of Biophysics Chinese Academy of Sciences Beijing 100101 China

NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular *** method has unique strengths and *** the two techniques are highly complementary,they have generally been used separately to address the structure and functions of biomolecular *** this review,we emphasize that the combination of NMR spectroscopy and X-ray crystallography offers unique power for elucidating the structures of complicated protein *** demonstrate,using several recent examples from our own laboratory,that the exquisite sensitivity of NMR spectroscopy in detecting the conformational properties of individual atoms in proteins and their complexes,without any prior knowledge of conformation,is highly valuable for obtaining the high quality crystals necessary for structure determination by X-ray *** NMR spectroscopy,in addition to answering many unique structural biology questions that can be addressed specifically by that technique,can be exceedingly powerful in modern structural biology when combined with other techniques including X-ray crystallography and cryo-electron microscopy.

关键词： NMR spectroscopy X-ray crystallography structural biology protein complex assembly

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Alb4 of Arabidopsis Promotes assembly and Stabilization of a Non Chlorophyll-Binding Photosynthetic complex, the CF1CF0-ATP Synthase

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Molecular Plant 2009年第6期2卷 1410-1424页

作者： Monique Benz Thomas Bals Irene Luise Gugel Markus Piotrowski Andreas Kuhn Danja Schunemann Jurgen Soll Elisabeth Ankele Department of Biologie I-Botanik Biozentrum Ludwig-Maximillians-University Munich Grosshadernerstrasse 2-4 D-82152 Planegg-Martinsried Germany Munich Centre for Integrated protein Science CIPSM Ludwig-Maximillians-University Munich Feodor-Lynen-Strasse 25 D-81377 Munich Germany Department of Plant Physiology Ruhr-University Bochum D-44780 Bochum Germany Department of Microbiology University of Hohenheim Garbenstrasse 30 D-70599 Hohenheim Germany

All members of the YidC/Oxal/Alb3 protein family are evolutionarily conserved and appear to function in membrane protein integration and protein complex stabilization. Here, we report on a second thylakoidal isoform of Alb3, named Alb4. Analysis of Arabidopsis knockout mutant lines shows that AIb4 is required in assembly and/or stability of the CF1CF0-ATP synthase （ATPase）. alb4 mutant lines not only have reduced steady-state levels of ATPase subunits, but also their assembly into high-molecular-mass complexes is altered, leading to a reduction of ATP synthesis in the mutants. Moreover, we show that Alb4 but not AIb3 physically interacts with the subunits CF1β and CF0ll. Summarizing, the data indicate that AIb4 functions to stabilize or promote assembly of CF1 during its attachment to the membrane-embedded CF0 part.

关键词： Alb4 Alb3 Arabidopsis thylakoid membrane protein insertion protein complex assembly CF1CF0-ATP synthase.

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Nucleus-Encoded Light-Harvesting Chlorophyll a/b proteins are Imported Normally into Chlorophyll b-Free Chloroplasts of Arabidopsis

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Molecular Plant 2013年第3期6卷 860-871页

作者： Sabine Nick Jorg Meurer Jurgen Soil Elisabeth Ankele Dept Biologie I-Botanik Biozentrum LMU Munchen Grosshadernerstrasse 2-4 D-82152 Planegg-Martinsried Germany Munich Center for Integrated protein Science ClPSM Ludwig-Maximilians-Universitat Munchen Feodor-Lynen-Strasse 25 D-81377 Munich Germany

Chloroplast-located proteins which are encoded by the nuclear genome have to be imported from the cytosol into the organelle in a posttranslational manner. Among these nuclear-encoded chloroplast proteins are the light- harvesting chlorophyll a/b-binding proteins （LHCPs）. After translation in the cytosol, precursor proteins of LHCPs are imported via the TOC/TIC translocase, processed to their mature size to insert into thylakoid membranes where they recruit chlorophylls a and b to form pigment-protein complexes. The translocation of proteins is a highly regulated process which employs several regulators. To analyze whether CAO （chlorophyll a oxigenase） which converts chlorophyll a to chlorophyll b at the inner chloroplast membrane, is one of these regulators, we performed import reactions utilizing a homozygous loss-of-function mutant （cao-1）. We imported in vitro translated and 35S-labeled precursor proteins of light- harvesting proteins of photosystem II LHCB1, LHCB4, and LHCB5 into chloroplasts isolated from cao-1 and show that import of precursor proteins and their processing to mature forms are not impaired in the mutant. Therefore, regulation of the import machinery cannot be responsible for the decreased steady-state levels of light-harvesting complex （LHC） proteins. Regulation does not take place at the transcriptional level either, because Lhcb mRNAs are not down-regulated. Additionally, reduced steady-state levels of LHCPs also do not occur due to posttranslational turnover of non-functional LHCPs in chloroplasts. Taken together, our data show that plants in the absence of CAO and therefore devoid of chlorophyll b are not influenced in their import behavior of LHC proteins.

关键词： chloroplast import LHCPs cao-1 protein complex assembly thylakoid membranes photosynthesis.

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Crystal Structure of the Elongator Subcomplex Elp4-6

Crystal Structure of the Elongator Subcomplex Elp4-6

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中国晶体学会第五届全国会员代表大会暨学术大会（大分子分会场）

作者： Zhijie Lin Weijing Zhao Wentao Diao Xingqiao Xie Zheng Wang Jinxiu Zhang Yuequan Shen Jiafu Long State Key Laboratory of Medicinal Chemical Biology College of Life Sciences Nankai University

Background: Elongator is a multiprotein complex that exhibits acetyltransferase activity. Results: In the subcomplex Elp4-6, Elp6 acts as a bridge to assemble Elp4 and Elp5, and each subunit adopts a similar RecA-ATPase-like fold. Conclusion: Subcomplex Elp4-6 formsa hexameric ring-shaped structure that is important for histone H3 binding. Significance: This finding may shed light on holo-Elongator complex assembly and its substrate recognition.

关键词： Elongator complex Elp4-6 protein complex assembly Ring-shaped Structure RNA Polymerase Ⅱ

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