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 |
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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 journal › Article
}
TY - JOUR
T1 - Regulation of ribozyme activity by engineered protein switch.
AU - Tanaka, Terumichi
AU - Kanda, Naomi
AU - Kikuchi, Yo
PY - 2005
Y1 - 2005
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=39049176450&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=39049176450&partnerID=8YFLogxK
M3 - Article
C2 - 17150774
AN - SCOPUS:39049176450
SP - 343
EP - 344
JO - Nucleic acids symposium series (2004)
JF - Nucleic acids symposium series (2004)
SN - 1746-8272
IS - 49
ER -