Yeast ribosomal protein S3 possesses a beta-lyase activity on damaged DNA
DC Field | Value | Language |
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dc.contributor.author | Seong, Ki Moon | - |
dc.contributor.author | Jung, Sang-Oun | - |
dc.contributor.author | Kim, Hag Dong | - |
dc.contributor.author | Kim, Hee Ju | - |
dc.contributor.author | Jung, You-Jin | - |
dc.contributor.author | Choi, Soo-Young | - |
dc.contributor.author | Kim, Joon | - |
dc.date.accessioned | 2021-09-06T08:39:23Z | - |
dc.date.available | 2021-09-06T08:39:23Z | - |
dc.date.created | 2021-06-19 | - |
dc.date.issued | 2012-02-17 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/105454 | - |
dc.description.abstract | Yeast ribosomal protein S3 has multifunctional activities that are involved in both protein translation and DNA repair. Here, we report that yeast Rps3p cleaves variously damaged DNA that contains not only AP sites and pyrimidine dimers but also 7,8-hydro-8-oxoguanine. This study also revealed that Rps3p has a beta-lyase activity with a broad range of substrate specificity which cleaves phosphodiester bonds of UV or oxidatively damaged DNA substrates. Mutation analysis of the yeast Rps3 protein including introduction of domain deletions and residue replacements identified the residues Asp154 and Lys200 are important for the catalytic activity. In addition, the repair enzyme activity of yeast Rps3p was confirmed by complementation in xth, nfo Escherichia coli cells in which the DNA repair process is defective. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | ENDONUCLEASE ACTIVITY | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | ENZYMATIC-ACTIVITY | - |
dc.subject | PURIFICATION | - |
dc.subject | CELLS | - |
dc.subject | CONTAINS | - |
dc.subject | RESIDUE | - |
dc.subject | RPS3 | - |
dc.title | Yeast ribosomal protein S3 possesses a beta-lyase activity on damaged DNA | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Joon | - |
dc.identifier.doi | 10.1016/j.febslet.2011.12.030 | - |
dc.identifier.scopusid | 2-s2.0-84862792992 | - |
dc.identifier.wosid | 000300588600012 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.586, no.4, pp.356 - 361 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 586 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 356 | - |
dc.citation.endPage | 361 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | ENDONUCLEASE ACTIVITY | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | ENZYMATIC-ACTIVITY | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | CONTAINS | - |
dc.subject.keywordPlus | RESIDUE | - |
dc.subject.keywordPlus | RPS3 | - |
dc.subject.keywordAuthor | Yeast Rps3p | - |
dc.subject.keywordAuthor | Lyase | - |
dc.subject.keywordAuthor | AP sites | - |
dc.subject.keywordAuthor | Pyrimidine dimer | - |
dc.subject.keywordAuthor | 8-Oxo-G | - |
dc.subject.keywordAuthor | DNA repair | - |
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