دورية أكاديمية
أعرض في EDS

Global kinetic mechanism describing single nucleotide incorporation for RNA polymerase I reveals fast UMP incorporation.

التفاصيل البيبلوغرافية
العنوان: Global kinetic mechanism describing single nucleotide incorporation for RNA polymerase I reveals fast UMP incorporation.
المؤلفون: Fuller KB; Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294, USA., Jacobs RQ; Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, AL 35294, USA., Carter ZI; Research, New England Biolabs, Ipswich, MA 01938, USA., Cuny ZG; Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294, USA., Schneider DA; Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, AL 35294, USA. Electronic address: dschneid@uab.edu., Lucius AL; Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294, USA. Electronic address: allucius@uab.edu.
المصدر: Biophysical chemistry [Biophys Chem] 2024 Sep; Vol. 312, pp. 107281. Date of Electronic Publication: 2024 Jun 08.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Science B.V Country of Publication: Netherlands NLM ID: 0403171 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-4200 (Electronic) Linking ISSN: 03014622 NLM ISO Abbreviation: Biophys Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier Science B.V
Original Publication: Amsterdam, North-Holland Pub. Co.
مواضيع طبية MeSH: RNA Polymerase I*/metabolism , RNA Polymerase I*/chemistry, Kinetics ; Nucleotides/metabolism ; Nucleotides/chemistry
مستخلص: RNA polymerase I (Pol I) is responsible for synthesizing ribosomal RNA, which is the rate limiting step in ribosome biogenesis. We have reported wide variability in the magnitude of the rate constants defining the rate limiting step in sequential nucleotide additions catalyzed by Pol I. in this study we sought to determine if base identity impacts the rate limiting step of nucleotide addition catalyzed by Pol I. To this end, we report a transient state kinetic interrogation of AMP, CMP, GMP, and UMP incorporations catalyzed by Pol I. We found that Pol I uses one kinetic mechanism to incorporate all nucleotides. However, we found that UMP incorporation is faster than AMP, CMP, and GMP additions. Further, we found that endonucleolytic removal of a dimer from the 3' end was fastest when the 3' terminal base is a UMP. It has been previously shown that both downstream and upstream template sequence identity impacts the kinetics of nucleotide addition. The results reported here show that the incoming base identity also impacts the magnitude of the observed rate limiting step.
Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: A.L.L. consults for Nitrase Therapeutics. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
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معلومات مُعتمدة: R35 GM140710 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: Enzyme kinetics; RNA polymerase I; Ribosomal RNA; Transcription; Transient-state kinetics
المشرفين على المادة: EC 2.7.7.6 (RNA Polymerase I)
0 (Nucleotides)
تواريخ الأحداث: Date Created: 20240618 Date Completed: 20240720 Latest Revision: 20240723
رمز التحديث: 20240723
مُعرف محوري في PubMed: PMC11260521
DOI: 10.1016/j.bpc.2024.107281
PMID: 38889653
قاعدة البيانات: MEDLINE
الوصف
تدمد:1873-4200
DOI:10.1016/j.bpc.2024.107281