作者: Kazufumi Takano , Tomohiro Okamoto , Jun Okada , Shun-ichi Tanaka , Clement Angkawidjaja
DOI: 10.1371/JOURNAL.PONE.0016226
关键词: C-terminus 、 Hyperthermophile 、 Sulfolobus 、 Sulfolobus tokodaii 、 Biochemistry 、 RNase P 、 Protein stabilization 、 Peptide sequence 、 RNase H 、 Chemistry 、 General Biochemistry, Genetics and Molecular Biology 、 General Agricultural and Biological Sciences 、 General Medicine
摘要: RNase HI from the hyperthermophile Sulfolobus tokodaii (Sto-RNase HI) is stabilized by its C-terminal residues. In this work, stabilization effect of Sto-RNase residues was investigated in detail thermodynamic measurements stability variants lacking disulfide bond (C58/145A), or six (ΔC6) and structural analysis ΔC6. The results showed that does not affect overall structure caused local interactions C-terminal, suggesting could be used as a “stabilization tag.” (-IGCIILT) were introduced tag on three proteins. Each chimeric protein more stable than wild-type protein. These suggested possibility simple technique using such