Thermodynamic Analysis of a Multifunctional RNA-Binding Protein, PhoRpp38, in the Hyperthermophilic Archaeon Pyrococcus horikoshii OT3

Autor:	Makoto Kimura, Kosuke Oshima, Kouhei Tsumoto, Yoshimitsu Kakuta, Takashi Nakashima
Rok vydání:	2012
Předmět:	biology Stereochemistry RNase P Organic Chemistry RNA Isothermal titration calorimetry RNA-binding protein General Medicine Applied Microbiology and Biotechnology biology.organism_classification Biochemistry Analytical Chemistry Pyrococcus horikoshii Molecular Biology Biotechnology Archaea
Zdroj:	Bioscience, Biotechnology, and Biochemistry. 76:1252-1255
ISSN:	1347-6947 0916-8451
DOI:	10.1271/bbb.120272
Popis:	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 × 107 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 7.0 A on a synchrotron X-ray source.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::3057cf4d0bdf426c90348a2d73e6920d https://doi.org/10.1271/bbb.120272 Zobrazit plný text záznamu