| http://purl.uniprot.org/citations/18721139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18721139 | http://www.w3.org/2000/01/rdf-schema#comment | "Eukaryotic ribonuclease (RNase) H2 consists of one catalytic and two accessory subunits. Several single mutations in any one of these subunits of human RNase H2 cause Aicardi-Goutières syndrome. To examine whether these mutations affect the complex stability and activity of RNase H2, three mutant proteins of His-tagged Saccharomyces cerevisiae RNase H2 (Sc-RNase H2*) were constructed. Sc-G42S*, Sc-L52R*, and Sc-K46W* contain single mutations in Sc-Rnh2Ap*, Sc-Rnh2Bp*, and Sc-Rnh2Cp*, respectively. The genes encoding the three subunits were coexpressed in Escherichia coli, and Sc-RNase H2* and its derivatives were purified in a heterotrimeric form. All of these mutant proteins exhibited enzymatic activity. However, only the enzymatic activity of Sc-G42S* was greatly reduced compared to that of the wild-type protein. Gly42 is conserved as Gly10 in Thermococcus kodakareansis RNase HII. To analyze the role of this residue, four mutant proteins, Tk-G10S, Tk-G10A, Tk-G10L, and Tk-G10P, were constructed. All mutant proteins were less stable than the wild-type protein by 2.9-7.6 degrees C in T(m). A comparison of their enzymatic activities, substrate binding affinities, and CD spectra suggests that the introduction of a bulky side chain into this position induces a local conformational change, which is unfavorable for both activity and substrate binding. These results indicate that Gly10 is required to make the protein fully active and stable."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1742-4658.2008.06622.x"xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/author | "Koga Y."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/author | "Kanaya S."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/author | "Takano K."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/author | "Chon H."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/author | "Crouch R.J."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/author | "Rohman M.S."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/name | "FEBS J"xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/pages | "4836-4849"xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/title | "Effect of the disease-causing mutations identified in human ribonuclease (RNase) H2 on the activities and stabilities of yeast RNase H2 and archaeal RNase HII."xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://purl.uniprot.org/core/volume | "275"xsd:string |
| http://purl.uniprot.org/citations/18721139 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18721139 |
| http://purl.uniprot.org/citations/18721139 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18721139 |
| http://purl.uniprot.org/uniprot/#_P53942-mappedCitation-18721139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18721139 |
| http://purl.uniprot.org/uniprot/#_Q05635-mappedCitation-18721139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18721139 |
| http://purl.uniprot.org/uniprot/#_Q12338-mappedCitation-18721139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18721139 |
| http://purl.uniprot.org/uniprot/Q12338 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/18721139 |
| http://purl.uniprot.org/uniprot/Q05635 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/18721139 |
| http://purl.uniprot.org/uniprot/P53942 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/18721139 |