Regulation of ribozyme activity by engineered protein switch.

Terumichi Tanaka; Naomi Kanda; Yo Kikuchi

Regulation of ribozyme activity by engineered protein switch.

Terumichi Tanaka^*, Naomi Kanda, Yo Kikuchi

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	343-344
Number of pages	2
Journal	Nucleic acids symposium series (2004)
Issue number	49
Publication status	Published - 2005
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Cite this

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title = "Regulation of ribozyme activity by engineered protein switch.",

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.",

author = "Terumichi Tanaka and Naomi Kanda and Yo Kikuchi",

year = "2005",

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AU - Kanda, Naomi

AU - Kikuchi, Yo

PY - 2005

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AB - 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.

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Regulation of ribozyme activity by engineered protein switch.

Abstract

ASJC Scopus subject areas

UN SDGs

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