Regulation of ribozyme activity by engineered protein switch.

Terumichi Tanaka, Naomi Kanda, Yo Kikuchi

Research output: Contribution to journalArticle

Abstract

Previously, we showed that the P3 domain of the Escherichia coli ribonuclease P ribozyme can be truncated and replaced in vitro. In this study, we prepared a P3-replaced variant of the E. coli ribozyme that has HIV TAR sequence as the engineered P3 domain. The mutant ribozyme demonstrated the ribonuclease P activity and was inhibited in the presence of the HIV tat protein fragment. Our results showed that the P3 domain of this enzyme can be engineered, and addition of some heterologous protein subunits can also be done to this domain.

Original languageEnglish
Pages (from-to)343-344
Number of pages2
JournalNucleic acids symposium series (2004)
Issue number49
Publication statusPublished - 2005
Externally publishedYes

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Catalytic RNA
Ribonuclease P
Human Immunodeficiency Virus tat Gene Products
Escherichia coli
Proteins
Protein Subunits
HIV
Enzymes

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Regulation of ribozyme activity by engineered protein switch. / Tanaka, Terumichi; Kanda, Naomi; Kikuchi, Yo.

In: Nucleic acids symposium series (2004), No. 49, 2005, p. 343-344.

Research output: Contribution to journalArticle

Tanaka, Terumichi ; Kanda, Naomi ; Kikuchi, Yo. / Regulation of ribozyme activity by engineered protein switch. In: Nucleic acids symposium series (2004). 2005 ; No. 49. pp. 343-344.
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