Structural highlights
Publication Abstract from PubMed
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 (DeltaC6) and by structural analysis of DeltaC6. 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.
Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag.,Takano K, Okamoto T, Okada J, Tanaka S, Angkawidjaja C, Koga Y, Kanaya S PLoS One. 2011 Jan 19;6(1):e16226. PMID:21283826[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takano K, Okamoto T, Okada J, Tanaka S, Angkawidjaja C, Koga Y, Kanaya S. Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag. PLoS One. 2011 Jan 19;6(1):e16226. PMID:21283826 doi:10.1371/journal.pone.0016226
