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Publication Abstract from PubMed

RNase HII exists ubiquitously in organisms and functions as a monomer in prokaryotes. We determined the crystal structure of Staphylococcus aureus RNase HII (Sa-RNase HII), which displays a novel dimer conformation, with the active site of each monomer covered by the other one. Both small-angle X-ray scattering and gel-filtration analysis confirmed that Sa-RNase HII exists as a homodimer in solution. Enzymatic analysis revealed that the "self-inhibited" dimeric form is catalytically active. Furthermore, continuous-wave electron paramagnetic resonance experiments clarified that the Sa-RNase HII dimer undergoes a large conformational change upon substrate binding, but remains a dimer to catalyze the reaction. Our structural and biochemical studies identified a novel functional dimer of Sa-RNase HII with distinct regulation mechanism for its catalytic activity.

Structural insights into a novel functional dimer of Staphylococcus aureus RNase HII.,Hang T, Zhang X, Wu M, Wang C, Ling S, Xu L, Gong Q, Tian C, Zhang X, Zang J Biochem Biophys Res Commun. 2018 Jul 10. pii: S0006-291X(18)31521-3. doi:, 10.1016/j.bbrc.2018.07.026. PMID:30005877^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.