Controlling Self‐Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme

Jones, D. Dafydd; Barker, Paul D.

doi:10.1002/anie.200463035

Cited by 15 publications

(8 citation statements)

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“…The K d values of Zn-PP and Cu-PP for cyt b 562 were 500 AE 80 nM and 100 AE 30 nM, respectively. These values are at least one order of magnitude higher than the K d values calculated for the oxidised hemeapo-cyt b 562 complex, 9,12 indicating that the affinity for Cu-PP and Zn-PP is lower but still relatively high in biological terms.…”

mentioning

confidence: 63%

“…The holo-cyt b 562 (with heme bound) shows an intense Soret band at 427 nm. 9,12 Changes in the axial ligand coordination of the cyt b 562 's Met7 and His102 amino acids to the Zn-PP and Cu-PP might account for the shift of the Soret band towards higher (Zn-PP) and lower (Cu-PP) wavelengths in comparison to the heme-cyt b 562 . In particular the Soret peak of the cyt b 562 -Cu-PP at 414 nm suggests a 5-coordinated Cu-PP complex 13 and the ratio e a /e b > 1 is evidence of coordination of the Cu-PP to a nitrogen acceptor.…”

mentioning

confidence: 99%

“…7 It can also be linked to other proteins so the functional centres are coupled. 9 Crucially, we have recently shown that cyt b 562 can be designed to bind non-biological surfaces such as gold in defined orientations through the introduction of a cysteine amino acid at specific points in the protein structure. 7 The introduction of a thiol group by exchanging an aspartate for cysteine at residue 50 (D50C) has proved particularly useful.…”

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confidence: 99%

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Redox tuning of cytochrome b562 through facile metal porphyrin substitution

et al. 2012

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confidence: 63%

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confidence: 99%

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Redox tuning of cytochrome b562 through facile metal porphyrin substitution

et al. 2012

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“…Nanohedra [19] and protein nanobuilding blocks [20,21]), split proteins/domains (e.g. Spycatcher [22] and split luciferase domains [23]), helix-helix interactions [24–26], metal ion bridging [27–29], cofactor bridging [30], and disulfide bridging [7] — to name a few [31–34].…”

Section: Designing Artificial Oligomersmentioning

confidence: 99%

Better together: building protein oligomers naturally and by design

Gwyther

Jones

Worthy

2019

Biochemical Society Transactions

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Protein oligomers are more common in nature than monomers, with dimers being the most prevalent final structural state observed in known structures. From a biological perspective, this makes sense as it conserves vital molecular resources that may be wasted simply by generating larger single polypeptide units, and allows new features such as cooperativity to emerge. Taking inspiration from nature, protein designers and engineers are now building artificial oligomeric complexes using a variety of approaches to generate new and useful supramolecular protein structures. Oligomerisation is thus offering a new approach to sample structure and function space not accessible through simply tinkering with monomeric proteins.

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“…Haem affinity for cyt b is oxidation state dependent, which potentially provides a way of monitoring cellular redox changes. Cyt b has been used previously to link redox-dependent haem binding events to other functions, such as DNA recognition (19,20). However, coupling haem binding to a reporter protein with an easily detected output would be advantageous.…”

Section: Introductionmentioning

confidence: 99%

Linking the functions of unrelated proteins using a novel directed evolution domain insertion method

Edwards

Busse

Allemann

et al. 2008

Nucleic Acids Research

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We have successfully developed a new directed evolution method for generating integral protein fusions comprising of one domain inserted within another. Creating two connections between the insert and accepting parent domain can result in the inter-dependence of the separate protein activities, thus providing a general strategy for constructing molecular switches. Using an engineered transposon termed MuDel, contiguous trinucleotide sequences were removed at random positions from the bla gene encoding TEM-1 β-lactamase. The deleted trinucleotide sequence was then replaced by a DNA cassette encoding cytochrome b562 with differing linking sequences at each terminus and sampling all three reading frames. The result was a variety of chimeric genes encoding novel integral fusion proteins that retained TEM-1 activity. While most of the tolerated insertions were observed in loops, several also occurred close to the termini of α-helices and β-strands. Several variants conferred a switching phenotype on Escherichia coli, with bacterial tolerance to ampicillin being dependent on the presence of haem in the growth medium. The magnitude of the switching phenotype ranged from 4- to 128-fold depending on the insertion position within TEM-1 and the linker sequences that join the two domains.

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Controlling Self‐Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme

Cited by 15 publications

References 36 publications

Redox tuning of cytochrome b562 through facile metal porphyrin substitution

Redox tuning of cytochrome b562 through facile metal porphyrin substitution

Better together: building protein oligomers naturally and by design

Linking the functions of unrelated proteins using a novel directed evolution domain insertion method

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