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
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