Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3

Kosuke Oshima, Takashi Nakashima, Yoshimitsu Kakuta, Kouhei Tsumoto, Makoto Kimura

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. Previous biochemical data indicate that it binds to two stem-loops in RNase P RNA (PhopRNA). Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56 × 10 7 M -1. It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA with approximately equal affinity. Crystals of PhoRpp38 in complex with the stem-loop were grown and diffracted to a resolution of 7.0Å on a synchrotron X-ray source.

Original languageEnglish
Pages (from-to)1252-1255
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Volume76
Issue number6
DOIs
Publication statusPublished - Jun 29 2012

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Pyrococcus horikoshii
Ribonuclease P
RNA-Binding Proteins
Archaea
Thermodynamics
Synchrotrons
X-Rays
RNA
X rays
Crystals
Proteins

All Science Journal Classification (ASJC) codes

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

Cite this

Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3. / Oshima, Kosuke; Nakashima, Takashi; Kakuta, Yoshimitsu; Tsumoto, Kouhei; Kimura, Makoto.

In: Bioscience, Biotechnology and Biochemistry, Vol. 76, No. 6, 29.06.2012, p. 1252-1255.

Research output: Contribution to journalArticle

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