Tag-mediated single-step purification and immobilization of recombinant proteins toward protein-engineered advanced materials

Freitas, Ana Isabel Costa; Domingues, Lucı́lia; Aguiar, Tatiana Quinta

doi:10.1016/j.jare.2021.06.010

Cited by 45 publications

(39 citation statements)

References 167 publications

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“…in vitro 18 . The magnetic property of MagR and MagR/Cry complex have been further confirmed theoretically 19 , 20 and experimentally 21 – 23 . Currently, there are four hypotheses have been proposed to explain the principle of animal magnetoreception: electromagnetic induction model 24 – 26 , magnetite model 27 – 32 , radical pair model based on cryptochrome (Cry) 33 – 40 and biocompass model based on MagR/Cry complex 18 , 41 .…”

Section: Introductionmentioning

confidence: 53%

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Guo

Chen

et al. 2021

Sci Rep

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Iron–sulfur clusters are essential cofactors found in all kingdoms of life and play essential roles in fundamental processes, including but not limited to respiration, photosynthesis, and nitrogen fixation. The chemistry of iron–sulfur clusters makes them ideal for sensing various redox environmental signals, while the physics of iron–sulfur clusters and its host proteins have been long overlooked. One such protein, MagR, has been proposed as a putative animal magnetoreceptor. It forms a rod-like complex with cryptochromes (Cry) and possesses intrinsic magnetic moment. However, the magnetism modulation of MagR remains unknown. Here in this study, iron–sulfur cluster binding in MagR has been characterized. Three conserved cysteines of MagR play different roles in iron–sulfur cluster binding. Two forms of iron–sulfur clusters binding have been identified in pigeon MagR and showed different magnetic properties: [3Fe–4S]-MagR appears to be superparamagnetic and has saturation magnetization at 5 K but [2Fe–2S]-MagR is paramagnetic. While at 300 K, [2Fe–2S]-MagR is diamagnetic but [3Fe–4S]-MagR is paramagnetic. Together, the different types of iron–sulfur cluster binding in MagR attribute distinguished magnetic properties, which may provide a fascinating mechanism for animals to modulate the sensitivity in magnetic sensing.

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Section: Introductionmentioning

confidence: 53%

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Guo

Chen

et al. 2021

Sci Rep

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“…A wide variety of tags are applied in biomolecule-mediated covalent immobilisation of enzymes directly from cell lysate with excellent precision and activity retention. [66][67][68][69][70] 4.1 Tag-mediated self-catalytic biorthogonal ligation 4.1.1 His-tag. Bio-orthogonal chemical immobilisation of an enzyme using the His-tag methodology enables the exposure of its bioactive domain to achieve optimum activity.…”

Section: Tag-mediated Bio-orthogonal Covalent Immobilisation Of Enzymesmentioning

confidence: 99%

Putting precision and elegance in enzyme immobilisation with bio-orthogonal chemistry

Pei

Luo

et al. 2022

Chem. Soc. Rev.

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“…Dehalogenases act as tags when genetically fused to a protein of interest, termed HaloTag technology (England et al, 2015;Döbber and Pohl, 2017;Erdmann et al, 2019). This technology overcomes the current limitations of traditional protein tagging platforms, as it can be applied to protein isolation and purification, studies of protein synthesis and degradation, analyses of protein function, studies of protein-protein and protein-DNA interactions, and molecular and cellular imaging (Encell et al, 2012;Merrill et al, 2019;Cattoglio et al, 2020;Freitas et al, 2021;Minner-Meinen et al, 2021). Furthermore, novel technologies have been developed for tumor diagnosis and treatment involving the linkage of dehalogenase fused with cancer cell recognition peptides to multifunctional nanoparticles (Garbujo et al, 2020).…”

Section: Other Fieldsmentioning

confidence: 99%

Mini Review: Advances in 2-Haloacid Dehalogenases

et al. 2021

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The 2-haloacid dehalogenases (EC 3.8.1.X) are industrially important enzymes that catalyze the cleavage of carbon–halogen bonds in 2-haloalkanoic acids, releasing halogen ions and producing corresponding 2-hydroxyl acids. These enzymes are of particular interest in environmental remediation and environmentally friendly synthesis of optically pure chiral compounds due to their ability to degrade a wide range of halogenated compounds with astonishing efficiency for enantiomer resolution. The 2-haloacid dehalogenases have been extensively studied with regard to their biochemical characterization, protein crystal structures, and catalytic mechanisms. This paper comprehensively reviews the source of isolation, classification, protein structures, reaction mechanisms, biochemical properties, and application of 2-haloacid dehalogenases; current trends and avenues for further development have also been included.

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Tag-mediated single-step purification and immobilization of recombinant proteins toward protein-engineered advanced materials

Abstract: Graphical abstract

Cited by 45 publications

References 167 publications

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Putting precision and elegance in enzyme immobilisation with bio-orthogonal chemistry

Mini Review: Advances in 2-Haloacid Dehalogenases

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