دورية أكاديمية
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A dedicated diribonucleotidase resolves a key bottleneck for the terminal step of RNA degradation.

التفاصيل البيبلوغرافية
العنوان: A dedicated diribonucleotidase resolves a key bottleneck for the terminal step of RNA degradation.
المؤلفون: Kim SK; Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, United States., Lormand JD; Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, United States., Weiss CA; Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, United States., Eger KA; Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, United States., Turdiev H; Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, United States., Turdiev A; Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, United States., Winkler WC; Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, United States., Sondermann H; Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, United States., Lee VT; Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, United States.
المصدر: ELife [Elife] 2019 Jun 21; Vol. 8. Date of Electronic Publication: 2019 Jun 21.
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: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: RNA Stability*, Bacterial Proteins/*metabolism , Exoribonucleases/*metabolism , Vibrio cholerae/*enzymology, Amino Acid Sequence ; Bacterial Proteins/chemistry ; Catalytic Domain ; Cyclic GMP/metabolism ; Exoribonucleases/chemistry ; Models, Biological ; Phenotype ; Pseudomonas aeruginosa/enzymology ; Pseudomonas aeruginosa/growth & development ; Ribonucleotides/metabolism ; Signal Transduction ; Substrate Specificity
مستخلص: Degradation of RNA polymers, an ubiquitous process in all cells, is catalyzed by specific subsets of endo- and exoribonucleases that together recycle RNA fragments into nucleotide monophosphate. In γ-proteobacteria, 3-'5' exoribonucleases comprise up to eight distinct enzymes. Among them, Oligoribonuclease (Orn) is unique as its activity is required for clearing short RNA fragments, which is important for cellular fitness. However, the molecular basis of Orn's unique cellular function remained unclear. Here, we show that Orn exhibits exquisite substrate preference for diribonucleotides. Crystal structures of substrate-bound Orn reveal an active site optimized for diribonucleotides. While other cellular RNases process oligoribonucleotides down to diribonucleotide entities, Orn is the one and only diribonucleotidase that completes the terminal step of RNA degradation. Together, our studies indicate RNA degradation as a step-wise process with a dedicated enzyme for the clearance of a specific intermediate pool, diribonucleotides, that affects cellular physiology and viability.
Competing Interests: SK, JL, CW, KE, HT, AT, WW, HS, VL No competing interests declared
(© 2019, Kim et al.)
التعليقات: Erratum in: Elife. 2022 Jan 28;11:. (PMID: 35088715)
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معلومات مُعتمدة: P30 GM124166 United States GM NIGMS NIH HHS; R01 AI142400 United States AI NIAID NIH HHS; LEE16G0 International Cystic Fibrosis Foundation; T32-GM080201 United States GM NIGMS NIH HHS; R01AI142400 International National Institute of Allergy and Infectious Diseases; P41 GM103485 United States GM NIGMS NIH HHS; R01AI110740 International National Institute of Allergy and Infectious Diseases; R01 GM123609 United States GM NIGMS NIH HHS; R01 AI110740 United States AI NIAID NIH HHS; T32 AI089621 United States AI NIAID NIH HHS; T32 GM080201 United States GM NIGMS NIH HHS; R01GM123609 United States GM NIGMS NIH HHS; MCB1051440 International National Science Foundation
فهرسة مساهمة: Keywords: Pseudomonas aeruginosa; Vibrio cholerae; diribonuclease; diribonucleotides; infectious disease; microbiology; oligoribonuclease
سلسلة جزيئية: PDB 6N6C; 6N6D; 6N6E; 6N6F; 6N6G; 6N6H; 6N6I; 6N6J; 6N6K
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Ribonucleotides)
EC 3.1.- (Exoribonucleases)
EC 3.1.- (oligoribonuclease)
H2D2X058MU (Cyclic GMP)
تواريخ الأحداث: Date Created: 20190622 Date Completed: 20200219 Latest Revision: 20220129
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC6613908
DOI: 10.7554/eLife.46313
PMID: 31225796
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.46313