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Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag
RNase HI from the hyperthermophile Sulfolobus tokodaii (Sto-RNase HI) is stabilized by its C-terminal residues. In this work, the stabilization effect of the Sto-RNase HI C-terminal residues was investigated in detail by thermodynamic measurements of the stability of variants lacking the disulfide b...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3023800/ https://www.ncbi.nlm.nih.gov/pubmed/21283826 http://dx.doi.org/10.1371/journal.pone.0016226 |
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author | Takano, Kazufumi Okamoto, Tomohiro Okada, Jun Tanaka, Shun-ichi Angkawidjaja, Clement Koga, Yuichi Kanaya, Shigenori |
author_facet | Takano, Kazufumi Okamoto, Tomohiro Okada, Jun Tanaka, Shun-ichi Angkawidjaja, Clement Koga, Yuichi Kanaya, Shigenori |
author_sort | Takano, Kazufumi |
collection | PubMed |
description | RNase HI from the hyperthermophile Sulfolobus tokodaii (Sto-RNase HI) is stabilized by its C-terminal residues. In this work, the stabilization effect of the Sto-RNase HI C-terminal residues was investigated in detail by thermodynamic measurements of the stability of variants lacking the disulfide bond (C58/145A), or the six C-terminal residues (ΔC6) and by structural analysis of ΔC6. The results showed that the C-terminal does not affect overall structure and stabilization is caused by local interactions of the C-terminal, suggesting that the C-terminal residues could be used as a “stabilization tag.” The Sto-RNase HI C-terminal residues (-IGCIILT) were introduced as a tag on three proteins. Each chimeric protein was more stable than its wild-type protein. These results suggested the possibility of a simple stabilization technique using a stabilization tag such as Sto-RNase HI C-terminal residues. |
format | Text |
id | pubmed-3023800 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-30238002011-01-31 Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag Takano, Kazufumi Okamoto, Tomohiro Okada, Jun Tanaka, Shun-ichi Angkawidjaja, Clement Koga, Yuichi Kanaya, Shigenori PLoS One Research Article RNase HI from the hyperthermophile Sulfolobus tokodaii (Sto-RNase HI) is stabilized by its C-terminal residues. In this work, the stabilization effect of the Sto-RNase HI C-terminal residues was investigated in detail by thermodynamic measurements of the stability of variants lacking the disulfide bond (C58/145A), or the six C-terminal residues (ΔC6) and by structural analysis of ΔC6. The results showed that the C-terminal does not affect overall structure and stabilization is caused by local interactions of the C-terminal, suggesting that the C-terminal residues could be used as a “stabilization tag.” The Sto-RNase HI C-terminal residues (-IGCIILT) were introduced as a tag on three proteins. Each chimeric protein was more stable than its wild-type protein. These results suggested the possibility of a simple stabilization technique using a stabilization tag such as Sto-RNase HI C-terminal residues. Public Library of Science 2011-01-19 /pmc/articles/PMC3023800/ /pubmed/21283826 http://dx.doi.org/10.1371/journal.pone.0016226 Text en Takano et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Takano, Kazufumi Okamoto, Tomohiro Okada, Jun Tanaka, Shun-ichi Angkawidjaja, Clement Koga, Yuichi Kanaya, Shigenori Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag |
title | Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag |
title_full | Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag |
title_fullStr | Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag |
title_full_unstemmed | Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag |
title_short | Stabilization by Fusion to the C-terminus of Hyperthermophile Sulfolobus tokodaii RNase HI: A Possibility of Protein Stabilization Tag |
title_sort | stabilization by fusion to the c-terminus of hyperthermophile sulfolobus tokodaii rnase hi: a possibility of protein stabilization tag |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3023800/ https://www.ncbi.nlm.nih.gov/pubmed/21283826 http://dx.doi.org/10.1371/journal.pone.0016226 |
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