Structural changes in ribonuclease P RNA in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 induced on interaction with proteins
Overview of Kosaka S et al.
| Authors | Kosaka S Hada K Nakashima T Kimura M |
|---|---|
| Affiliation | Laboratory of Structural Biology Graduate School of Systems Life Sciences Kyushu University Fukuoka Japan. |
| Journal | Biosci Biotechnol Biochem |
| Year | 2010 |
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.