Activating an Enzyme by an Engineered Coiled Coil Switch

Yuzawa, Satoshi; Mizuno, Toshihisa; Tanaka, Toshiki

doi:10.1002/chem.200600007

Cited by 16 publications

(13 citation statements)

References 39 publications

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“…Coiled-coils have seen a diverse array of applications in biomaterials, affinity purification, assembly of bispecific or high avidity antibodies, and reconstitution of various split proteins or dimerizationdependent protein complexes 29,30 . Conditionally dimeric coiled-coil fusions have previously been used to reconstitute and control a split mutant of RNAse T1 31 and to conditionally enact DNA binding by a bZIP domain upon photostimulation 32 .…”

Section: Discussionmentioning

confidence: 99%

Modular Thermal Control of Protein Dimerization

Piraner

Shapiro

2019

Preprint

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Protein-protein interactions and protein localization are essential mechanisms of cellular signal transduction. The ability to externally control such interactions using chemical and optogenetic methods has facilitated biological research and provided components for the engineering of cell-based therapies and materials. However, chemical and optical methods are limited in their ability to provide spatiotemporal specificity in light-scattering tissues. To overcome these limitations, we present "thermomers," modular protein dimerization domains controlled with temperature -a form of energy that can be delivered to cells both globally and locally in a wide variety of in vitro and in vivo contexts. Thermomers are based on a sharply thermolabile coiled-coil protein, which we engineered to heterodimerize at a tunable transition temperature within the biocompatible range of 37-42 ºC. When fused to other proteins, thermomers can reversibly control their association, as demonstrated via membrane localization in mammalian cells. This technology enables remote control of intracellular protein-protein interactions with a form of energy that can be delivered with spatiotemporal precision in a wide range of biological, therapeutic and living material scenarios.

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Section: Discussionmentioning

confidence: 99%

Modular Thermal Control of Protein Dimerization

Piraner

Shapiro

2019

Preprint

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“…Tanaka and colleagues inserted two out of three helices from a hetero-specific coiled-coil trimer into a circularly permuted version of RNaseT1. They showed that adding the missing helix could constitute the trimer, and with it the enzyme [30]. Reversible photo-activation of coiled-coil transcription factor binding to DNA has also been demonstrated [31].…”

Section: Novel Structures Switches and Functionsmentioning

confidence: 99%

Structural specificity in coiled-coil interactions

Grigoryan

Keating

2008

Current Opinion in Structural Biology

267

283

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Coiled coils have a rich history in the field of protein design and engineering. Novel structures, such as the first 7-helix coiled coil, continue to provide surprises and insights. Large-scale data sets quantifying the influence of systematic mutations on coiled-coil stability are a valuable new asset to the area. Scoring methods based on sequence and/or structure can predict interaction preferences in coiled-coil-mediated bZIP transcription factor dimerization. Experimental and computational methods for dealing with the near-degeneracy of many coiled-coil structures appear promising for future design applications.

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“…15–17 Specific examples of Ar-containing de novo and engineered CCs include: engineered pentameric barrels containing buried Trp or Phe residues (Figure 1C), 20,21 and heterotrimeric CCs with a buried Trp. 22–24 More recent examples include various parallel and antiparallel helical bundles with consolidated cores that feature Phe residues, 25–27 and homomeric and heteromeric helix-loop-helix motifs with isolated Tyr, His and Trp residues that contribute to buried hydrogen-bond networks (Figure 1D & E). 14…”

Section: Figurementioning

confidence: 99%

How coiled-coil assemblies accommodate multiple aromatic residues

Rhys

Dawson

Beesley

et al. 2021

Preprint

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Rational protein design requires understanding the contribution of each amino acid to a targeted protein fold. For a subset of protein structures, namely the α-helical coiled coils (CCs), knowledge is sufficiently advanced to allow the rational de novo design of many structures, including entirely new protein folds. However, current CC design rules center on using aliphatic hydrophobic residues predominantly to drive the folding and assembly of amphipathic α helices. The consequences of using aromatic residues--which would be useful for introducing structural probes, and binding and catalytic functionalities--into these interfaces is not understood. There are specific examples of de-signed CCs containing such aromatic residues, e.g., phenylalanine-rich sequences, and the use of polar aromatic resi-dues to make buried hydrogen-bond networks. However, it is not known generally if sequences rich in tyrosine can form CCs, or what CC assemblies these would lead to. Here we explore tyrosine-rich sequences in a general CC-forming background and resolve new CC structures. In one of these, an antiparallel tetramer, the tyrosine residues are solvent accessible and pack at the interface between the core and the surface. In the other more-complex structure, the residues are buried and form an extended hydrogen-bond network.

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Activating an Enzyme by an Engineered Coiled Coil Switch

Cited by 16 publications

References 39 publications

Modular Thermal Control of Protein Dimerization

Modular Thermal Control of Protein Dimerization

Structural specificity in coiled-coil interactions

How coiled-coil assemblies accommodate multiple aromatic residues

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