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...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3023800?pdf=render |
| _version_ | 1819102626690629632 |
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| author | Kazufumi Takano Tomohiro Okamoto Jun Okada Shun-ichi Tanaka Clement Angkawidjaja Yuichi Koga Shigenori Kanaya |
| author_facet | Kazufumi Takano Tomohiro Okamoto Jun Okada Shun-ichi Tanaka Clement Angkawidjaja Yuichi Koga Shigenori Kanaya |
| author_sort | Kazufumi Takano |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-22T01:37:33Z |
| format | Article |
| id | doaj.art-ea576ea4455940069ac69e201bd47a64 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T01:37:33Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-ea576ea4455940069ac69e201bd47a642022-12-21T18:43:20ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0161e1622610.1371/journal.pone.0016226Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag.Kazufumi TakanoTomohiro OkamotoJun OkadaShun-ichi TanakaClement AngkawidjajaYuichi KogaShigenori KanayaRNase 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.http://europepmc.org/articles/PMC3023800?pdf=render |
| spellingShingle | Kazufumi Takano Tomohiro Okamoto Jun Okada Shun-ichi Tanaka Clement Angkawidjaja Yuichi Koga Shigenori Kanaya Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag. PLoS ONE |
| 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 |
| url | http://europepmc.org/articles/PMC3023800?pdf=render |
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