The catalytic domain of the calcium-dependent endoribonuclease EndoU from Homo sapiens was expressed in E. coli with C and N labeling. A nearly complete assignment of backbone H, N, and C resonances was obtained, as well as a secondary structure prediction based on the assigned chemical shifts. The predicted secondary structures were almost identical to the published crystal structure of calcium-activated EndoU. This is the first NMR study of an eukaryotic member of the EndoU-like superfamily of ribonucleases.
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http://dx.doi.org/10.1007/s12104-024-10198-y | DOI Listing |
Biomol NMR Assign
December 2024
Univ. Bordeaux, CNRS, INSERM, ARNA, UMR 5320, U1212, Bordeaux, F-33000, France.
The catalytic domain of the calcium-dependent endoribonuclease EndoU from Homo sapiens was expressed in E. coli with C and N labeling. A nearly complete assignment of backbone H, N, and C resonances was obtained, as well as a secondary structure prediction based on the assigned chemical shifts.
View Article and Find Full Text PDFCurr Biol
December 2014
Cell Biology Section, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Building 35, Room 2C-913, 9000 Rockville Pike, Bethesda, MD 20892-3738, USA. Electronic address:
Endoplasmic reticulum (ER) sheet membranes are covered with ribosomes and RNAs that are involved in protein synthesis. A new study reveals that a calcium-activated endoribonuclease of the EndoU protein family promotes the formation of tubular ER networks, contributing to dynamic shaping of the ER in cells.
View Article and Find Full Text PDFJ Cell Biol
October 2014
Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114 Department of Genetics, Harvard Medical School, Boston, MA 02115
How cells shape and remodel organelles in response to cellular signals is a poorly understood process. Using Xenopus laevis egg extract, we found that increases in cytosolic calcium lead to the activation of an endogenous ribonuclease, XendoU. A fraction of XendoU localizes to the endoplasmic reticulum (ER) and is required for nuclear envelope assembly and ER network formation in a catalysis-dependent manner.
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