Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
RNA Epitranscriptomics & Proteomics Resource, University at Albany, State University of New York, Albany, New York 12222, United States.
J Phys Chem B. 2024 Jul 25;128(29):7002-7021. doi: 10.1021/acs.jpcb.4c00628. Epub 2024 Jul 16.
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.
核糖体结合许多代谢酶并改变它们的活性。为糖酵解酶磷酸丙糖异构酶（TPI）制定并阐明了一种核糖体介导的代谢酶活性放大的通用机制，即 RAMBO。RAMBO 效应源于核糖体依赖性电场-底物偶极相互作用能，它可以增加或减少反应物和产物的基态，从而调节催化速率。NMR 光谱用于确定 TPI 与核糖体结合的相互作用表面，并在不存在和存在完整核糖体颗粒的情况下测量相应的动力学速率。化学交联和质谱揭示了 TPI 与核糖体蛋白的潜在结合伙伴。结构结果以及 TPI 能量和活性的相关变化表明，TPI 与核糖体蛋白 L11 之间的相互作用介导了 RAMBO 效应。
