Structural changes in ribonuclease P RNA in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 induced on interaction with proteins.
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.
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University, Fukuoka, Japan.
Shunsuke
S
Kosaka
Kazumasa
K
Hada
Takashi
T
Nakashima
Makoto
M
Kimura
D001105:Archaea / Q000235:genetics / Q000378:metabolism*; D002942:Circular Dichroism; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D043902:Pyrococcus horikoshii / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012313:RNA / Q000235:genetics / Q000378:metabolism; D043262:Ribonuclease P / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D011506:Proteins; D012313:RNA; D043262:Ribonuclease P