Structural changes in ribonuclease P RNA in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 induced on interaction with proteins.

نویسندگان

  • Shunsuke Kosaka
  • Kazumasa Hada
  • Takashi Nakashima
  • Makoto Kimura
چکیده

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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Identification of nucleotide residues essential for RNase P activity from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.

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عنوان ژورنال:
  • Bioscience, biotechnology, and biochemistry

دوره 74 2  شماره 

صفحات  -

تاریخ انتشار 2010