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

Shunsuke Kosaka, Kazumasa Hada, Takashi Nakashima, Makoto Kimura

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The activated structure of RNase P RNA (PhopRNA) in Pyrococcus horikoshii OT3 was characterized by circular dichroism (CD) and ultraviolet (UV) absorb- ance 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.

Original languageEnglish
Pages (from-to)394-396
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume74
Issue number2
DOIs
Publication statusPublished - Mar 1 2010

Fingerprint

Pyrococcus horikoshii
Ribonuclease P
Archaea
RNA
Circular Dichroism
Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Analytical Chemistry
  • Organic Chemistry

Cite this

Structural changes in ribonuclease P RNA in the hyperthermophilic archaeon pyrococcus horikoshii OT3 induced on interaction with proteins. / Kosaka, Shunsuke; Hada, Kazumasa; Nakashima, Takashi; Kimura, Makoto.

In: Bioscience, Biotechnology and Biochemistry, Vol. 74, No. 2, 01.03.2010, p. 394-396.

Research output: Contribution to journalArticle

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