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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
Published on: February 12, 2022
Structural changes in ribonuclease P RNA in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 induced on
Shunsuke Kosaka1, Kazumasa Hada, Takashi Nakashima
1Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University, Fukuoka, Japan.
Abstract:
The activated structure of RNase P RNA (PhopRNA) in Pyrococcus horikoshii OT3 was characterized by circular dichroism (CD) and ultraviolet (UV) absorbance spectra. The results suggested that interaction of four RNase P proteins (PhoPop5, PhoRpp21, PhoRpp29, and PhoRpp30) with PhopRNA results in destabilization of base stacking in PhopRNA, whereas the addition of a fifth protein, PhoRpp38, increases base stacking in PhopRNA.
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