Sensing Cooperativity in ATP Hydrolysis for Single Multisubunit Enzymes in Solution

Jiang, Yan; Douglas, Nicholai R.; Conley, Nicholas R.; Miller, Erik J.; Frydman, Judith; Moerner, W. E.

doi:10.1016/j.bpj.2011.11.967

Cited by 17 publications

(28 citation statements)

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“…One possibility is that one octameric ring within a TriC complex is fully occupied by nucleotides whereas the other ring is empty. However, biochemical data presented in this study (2) and elsewhere indicate that each of the two rings contains four nucleotides each, a finding without a precedent in chaperonins.…”

Section: Standard Models Thatcontrasting

confidence: 53%

“…Another important feature of this scheme is its size dependence: because Cy3-ADP diffuses too quickly for the trap to follow, free Cy3-ADP released from TriC does not interfere with the enumeration of photobleaching steps. By using this approach, Jiang et al (2) are able to determine how many ADPs remain bound to the TriC complex as a function of time, to determine the time course of ADP release, and more importantly, to compile the entire distribution of the number of ADPs bound to each TriC complex. The ADP number distribution is narrowly peaked at eight.…”

Section: Commentarymentioning

confidence: 99%

“…Such multisubunit proteins represent major challenges and opportunities in developing new experimental approaches and theoretical framework needed to comprehend their interworking. In PNAS, Jiang et al (2) take a major step toward this goal by devising a unique single-molecule technique to analyze the conformational states of a single multisubunit enzyme.…”

mentioning

confidence: 99%

“…Jiang et al (2) provide just that by measuring the entire distribution of the number of nucleotides bound by a single multisubunit enzyme, the type 2 chaperonin called TriC. The mammalian TriC is made of two back-to-back rings, each ring consisting of eight different but related proteins.…”

mentioning

confidence: 99%

“…In all, there are 16 ATP binding sites in one TriC, but how many of these 16 binding sites are occupied by ATP? By using a fluorophore-labeled ADP (Cy3-ADP) and single-molecule confocal fluorescence microscopy, Jiang et al (2) detect single TriC complexes and observe the stepwise decreases in the fluorescence intensity caused by photobleaching (Fig. 1).…”

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confidence: 99%

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A single-molecule view of chaperonin cooperativity

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Section: Standard Models Thatcontrasting

confidence: 53%

Section: Commentarymentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Recent advancement of light‐based single‐molecule approaches for studying biomolecules

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et al. 2019

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Recent advances in single‐molecule techniques have led to new discoveries in analytical chemistry, biophysics, and medicine. Understanding the structure and behavior of single biomolecules provides a wealth of information compared to studying large ensembles. However, developing single‐molecule techniques is challenging and requires advances in optics, engineering, biology, and chemistry. In this paper, we will review the state of the art in single‐molecule applications with a focus over the last few years of development. The advancements covered will mainly include light‐based in vitro methods, and we will discuss the fundamentals of each with a focus on the platforms themselves. We will also summarize their limitations and current and future applications to the wider biological and chemical fields. This article is categorized under: Laboratory Methods and Technologies > Imaging Laboratory Methods and Technologies > Macromolecular Interactions, Methods Analytical and Computational Methods > Analytical Methods

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Super-Resolution Microscopy: From Single Molecules to Supramolecular Assemblies

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et al. 2015

Trends in Cell Biology

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Super-resolution microscopy (SRM) methods have allowed scientists to exceed the diffraction limit of light, enabling the discovery and investigation of cellular structures at the nanometer scale, from individual proteins to entire organelles. In this review we survey the application of SRM in elucidating the structure of macromolecules in the native cellular environment. We emphasize how SRM can generate molecular maps of protein complexes and extract quantitative information on the number, size, distribution, and spatial organization of macromolecules. We discuss both the novel information that can be generated through SRM as well as the experimental considerations to examine while conducting such studies. With the increasing popularity of SRM in the biological sciences, this review will serve as a tool to navigate the range of applications and harness the power of SRM to elucidate biological structures.

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Sensing Cooperativity in ATP Hydrolysis for Single Multisubunit Enzymes in Solution

Cited by 17 publications

References 0 publications

A single-molecule view of chaperonin cooperativity

A single-molecule view of chaperonin cooperativity

Recent advancement of light‐based single‐molecule approaches for studying biomolecules

Super-Resolution Microscopy: From Single Molecules to Supramolecular Assemblies

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