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Comparison List

mMaple

mMaple is a photoconvertible green fluorescent protein published in 2012, derived from Clavularia sp.. It has high acid sensitivity.
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Oligomerization Organism Molecular Weight Cofactor
Monomer Clavularia sp. 27.2 kDa -

Attributes

State Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
Green 489 505 15,000 0.74 11.1 8.2    
Red 566 583 30,000 0.56 16.8 7.3    

Transitions

From To Switch λ
Green Red 380

Photostability

no photostability measurements available ... add one!

mMaple Sequence

mMaple was derived from mClavGR2 with the following mutations: A183V/G209S/H259_P263delinsRNSTD/G264S
amino acid numbers relative to cFP484. show relative to mClavGR2

MVSKGEETIMSVIKPDMKIKLRMEGNVNGHAFVIEGEGSGKPFEGIQTIDLEVKEGAPLPFAYDILTTAFHYGNRVFTKYPEDIPDYFKQSFPEGYSWERSMTYEDGGICIATNDITMEEDSFINKIHFKGTNFPPNGPVMQKRTVGWEVSTEKMYVRDGVLKGDVKMKLLLKGGSHYRCDFRTTYKVKQKAVKLPDYHFVDHRIEILSHDKDYNKVKLYEHAVARNSTDSMDELYK
GenBank: ASA47684
IPG: 152367004

Excerpts

Single pcFP counting in individual bacterial cells by PALM/STORM reveals that a key contributor to the favorable properties of mMaple is a high intracellular concentration of properly folded (and therefore photoconvertible) mMaple fusion proteins.

McEvoy et al. (2012)

When the brightness of a large population of cells was assessed by flow cytometry, it was apparent that mMaple-actin or mMaple-actinin was not brighter than either of the corresponding mEos2 or mClavGR2 fusions when expressed in mammalian cells. For the actinin fusion, mClavGR2 had the greatest fraction of bright cells, followed by mMaple and mEos2. For the actin fusion, mClavGR2 and mEos2 had similar distributions that were shifted towards higher brightness relative to mMaple... Although these results were disappointing, we noted that the photostability of mMaple-actin is improved by almost three-fold, increasing the utility of the mMaple-actin construct in applications requiring green-state photostability.

McEvoy et al. (2012)

... we compared the relative signaling efficiency of different PAFPs by determining the number of single-molecule localizations per cell of the PAFPs fused to a common target protein under endogenous expression. We fused the PAFPs to the E. coli gene hupA, which encodes a subunit of the nucleoid-associated protein HU, at its endogenous chromosomal locus and determined the total number of HU-PAFP localizations per cell. Among the red PAFPs, mMaple provided by far the largest number of HU localizations, which was 6- to 32-fold higher than those of other HU-PAFP fusion proteins.

Wang et al. (2014)

We first took inspiration from the two mutations that make mEos3.2 more monomeric than mEos2: I102N and Y189A (15). Based on a sequence alignment between mEos2 and mMaple, we made the comparable mutations, I111N and Y198A, in mMaple... mMaple2 exhibited a similar photon budget, on–off ratio, and signaling efficiency as those of mMaple. ClpP-mMaple2 proteins still formed puncta in some cells. However, the percentage of cells showing single punctum was significantly reduced in comparison with ClpP-mMaple, suggesting a lower dimerization tendency of mMaple2.

Wang et al. (2014)

Primary Reference

Additional References

  1. Characterization and development of photoactivatable fluorescent proteins for single-molecule-based superresolution imaging

    Wang S, Moffitt Jr, Dempsey Gt, Xie Xs, Zhuang X

    (2014). Proceedings of the National Academy of Sciences, 111(23) , 8452-8457. doi: 10.1073/pnas.1406593111. Article   Pubmed

External Resources

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