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Ribosome External Electric Field Regulates Metabolic Enzyme Activity: The RAMBO Effect.
Yu, Jianchao; Ramirez, Lisa M; Lin, Qishan; Burz, David S; Shekhtman, Alexander.
Afiliação
  • Yu J; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
  • Ramirez LM; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
  • Lin Q; RNA Epitranscriptomics & Proteomics Resource, University at Albany, State University of New York, Albany, New York 12222, United States.
  • Burz DS; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
  • Shekhtman A; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
J Phys Chem B ; 128(29): 7002-7021, 2024 Jul 25.
Article em En | MEDLINE | ID: mdl-39012038
ABSTRACT
Ribosomes bind to many metabolic enzymes and change their activity. A general mechanism for ribosome-mediated amplification of metabolic enzyme activity, RAMBO, was formulated and elucidated for the glycolytic enzyme triosephosphate isomerase, TPI. The RAMBO effect results from a ribosome-dependent electric field-substrate dipole interaction energy that can increase or decrease the ground state of the reactant and product to regulate catalytic rates. NMR spectroscopy was used to determine the interaction surface of TPI binding to ribosomes and to measure the corresponding kinetic rates in the absence and presence of intact ribosome particles. Chemical cross-linking and mass spectrometry revealed potential ribosomal protein binding partners of TPI. Structural results and related changes in TPI energetics and activity show that the interaction between TPI and ribosomal protein L11 mediate the RAMBO effect.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ribossomos / Triose-Fosfato Isomerase Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ribossomos / Triose-Fosfato Isomerase Idioma: En Ano de publicação: 2024 Tipo de documento: Article