دورية أكاديمية
Yeast DNA diesterase for 3'-fragments of deoxyribose: purification and physical properties of a repair enzyme for oxidative DNA damage.
| العنوان: | Yeast DNA diesterase for 3'-fragments of deoxyribose: purification and physical properties of a repair enzyme for oxidative DNA damage. |
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| المؤلفون: | Johnson AW; Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138., Demple B |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 1988 Dec 05; Vol. 263 (34), pp. 18009-16. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | DNA Damage* , DNA Repair*, Endodeoxyribonucleases/*isolation & purification , Saccharomyces cerevisiae/*enzymology, Cations, Divalent ; Deoxyribose ; Endodeoxyribonucleases/metabolism ; Enzyme Stability ; Kinetics ; Molecular Weight ; Oxidation-Reduction ; Substrate Specificity ; Thermodynamics |
| مستخلص: | The DNA strand breaks resulting from exposure to the free radicals generated by ionizing radiation or oxidizing agents are refractory to DNA repair synthesis because of deoxyribose fragments that block their 3' termini. The restoration of normal 3'-OH nucleotide primers is the essential first step in the excision repair of these radical-induced strand breaks. We have used a synthetic DNA substrate containing 3'-phosphoglycolaldehyde esters to identify and purify to physical homogeneity the major yeast diesterase that removes such nucleotide fragments. Yeast 3'-phosphoglycolaldehyde diesterase had Mr = 40,500 upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A similar molecular weight estimate from gel filtration indicated that the active species is a nearly globular monomer. Purification of the enzyme removed a tightly bound metal, but the activity of the purified enzyme could be restored by the addition of Co2+, Mn2+, Ni2+, or Zn2+, with Co2+ the most effective cofactor. Even 3 microM Co2+ stimulated near-maximal activity, and this metal also conferred significant thermal stability on the purified protein. This is a novel enzyme, whose N-terminal amino acid sequence does not show any significant similarity to published sequences, and which is not the product of any gene in the RAD52 epistasis group. |
| معلومات مُعتمدة: | ES03926 United States ES NIEHS NIH HHS; GM07598 United States GM NIGMS NIH HHS |
| المشرفين على المادة: | 0 (Cations, Divalent) 533-67-5 (Deoxyribose) EC 3.1.- (Endodeoxyribonucleases) EC 3.1.25.- (3'-phosphoglycoaldehyde diesterase) |
| تواريخ الأحداث: | Date Created: 19881205 Date Completed: 19890103 Latest Revision: 20210318 |
| رمز التحديث: | 20240513 |
| PMID: | 3056935 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9258 |
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