دورية أكاديمية
أعرض في EDS

Structural Basis for Finding OG Lesions and Avoiding Undamaged G by the DNA Glycosylase MutY.

التفاصيل البيبلوغرافية
العنوان: Structural Basis for Finding OG Lesions and Avoiding Undamaged G by the DNA Glycosylase MutY.
المؤلفون: Russelburg LP; School of Biological Sciences , University of Utah , 257 South 1400 East , Salt Lake City , Utah 84112 , United States., O'Shea Murray VL; Department of Chemistry , University of California , Davis , California 95616 , United States.; Department of Chemistry , University of Utah , 315 South 1400 East , Salt Lake City , Utah 84112 , United States., Demir M; Department of Chemistry , University of California , Davis , California 95616 , United States., Knutsen KR; School of Biological Sciences , University of Utah , 257 South 1400 East , Salt Lake City , Utah 84112 , United States., Sehgal SL; School of Biological Sciences , University of Utah , 257 South 1400 East , Salt Lake City , Utah 84112 , United States., Cao S; Department of Chemistry , University of California , Davis , California 95616 , United States., David SS; Department of Chemistry , University of California , Davis , California 95616 , United States., Horvath MP; School of Biological Sciences , University of Utah , 257 South 1400 East , Salt Lake City , Utah 84112 , United States.
المصدر: ACS chemical biology [ACS Chem Biol] 2020 Jan 17; Vol. 15 (1), pp. 93-102. Date of Electronic Publication: 2019 Dec 27.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101282906 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1554-8937 (Electronic) Linking ISSN: 15548929 NLM ISO Abbreviation: ACS Chem Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c2006-
مواضيع طبية MeSH: DNA/*chemistry , DNA Glycosylases/*metabolism , DNA Repair/*drug effects , Targeted Gene Repair/*methods, Amino Acid Sequence ; Base Pair Mismatch ; Catalytic Domain ; Guanine/chemistry ; Kinetics ; Molecular Conformation ; Structure-Activity Relationship ; Substrate Specificity
مستخلص: The adenine glycosylase MutY selectively initiates repair of OG:A lesions and, by comparison, avoids G:A mispairs. The ability to distinguish these closely related substrates relies on the C-terminal domain of MutY, which structurally resembles MutT. To understand the mechanism for substrate specificity, we crystallized MutY in complex with DNA containing G across from the high-affinity azaribose transition state analogue. Our structure shows that G is accommodated by the OG site and highlights the role of a serine residue in OG versus G discrimination. The functional significance of Ser308 and its neighboring residues was evaluated by mutational analysis, revealing the critical importance of a β loop in the C-terminal domain for mutation suppression in cells, and biochemical performance in vitro . This loop comprising residues Phe307, Ser308, and His309 ( Geobacillus stearothermophilus sequence positions) is conserved in MutY but absent in MutT and other DNA repair enzymes and may therefore serve as a MutY-specific target exploitable by chemical biological probes.
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معلومات مُعتمدة: T32 GM008537 United States GM NIGMS NIH HHS; R01 CA067985 United States CA NCI NIH HHS; P30 GM124169 United States GM NIGMS NIH HHS; S10 OD018483 United States OD NIH HHS; T32 CA093247 United States CA NCI NIH HHS; R29 CA067985 United States CA NCI NIH HHS
المشرفين على المادة: 5Z93L87A1R (Guanine)
9007-49-2 (DNA)
EC 3.2.2.- (DNA Glycosylases)
EC 3.2.2.- (mutY adenine glycosylase)
تواريخ الأحداث: Date Created: 20191213 Date Completed: 20210113 Latest Revision: 20210118
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC7069122
DOI: 10.1021/acschembio.9b00639
PMID: 31829624
قاعدة البيانات: MEDLINE
الوصف
تدمد:1554-8937
DOI:10.1021/acschembio.9b00639