The chloroplast proteins cpSRP43 and cpSRP54 function in this chaperone role for the light-harvesting proteins. “Deciphering the three-dimensional structure of the core complex of these two proteins allows us to draw basic conclusions about how the chaperone functions”, explains Prof. Dr. Irm¬gard Sinning of the Heidelberg University Biochemistry Center (BZH). The team of scientists working with Prof. Sinning discovered that two protein motifs take part in the interaction between cpSRP43 and cpSRP54, similar to the motifs that play a central role in regulating access to the genetic material in the cell nucleus. While scientists have known for years about the “histone code” involved in the processes in the nucleus, they now face the puzzle of the newly discovered “arginine code” in the chloroplasts.The Heidelberg scientists conducted their research in close cooperation with colleagues from the Munich Technical University and the European Synchrotron Radiation Facility (ESRF) in Grenoble (France). The researchers combined different structural biology methods in the pursuit of their work. X-ray structure analysis, nuclear magnetic resonance (NMR) spectroscopy, and small angle X-ray scattering were key in revealing the architecture and dynamics of the core complex of cpSRP43 und cpSRP54. In addition, they took advantage of the Biochemistry Center’s protein crystallization platform, which receives support from the Cluster of Excellence CellNetworks at Heidelberg University. The results of the research were published in “Nature Structural & Molecular Biology”.
Marietta Fuhrmann-Koch | idw
Climate Impact Research in Hannover: Small Plants against Large Waves
17.08.2018 | Leibniz Universität Hannover
First transcription atlas of all wheat genes expands prospects for research and cultivation
17.08.2018 | Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung
New design tool automatically creates nanostructure 3D-print templates for user-given colors
Scientists present work at prestigious SIGGRAPH conference
Most of the objects we see are colored by pigments, but using pigments has disadvantages: such colors can fade, industrial pigments are often toxic, and...
Scientists at the University of California, Los Angeles present new research on a curious cosmic phenomenon known as "whistlers" -- very low frequency packets...
Scientists develop first tool to use machine learning methods to compute flow around interactively designable 3D objects. Tool will be presented at this year’s prestigious SIGGRAPH conference.
When engineers or designers want to test the aerodynamic properties of the newly designed shape of a car, airplane, or other object, they would normally model...
Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
Global demand for electric vehicles is forecast to rise sharply: by 2025, the number of new vehicle registrations is expected to reach 25 million per year....
Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...
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