Maturation efficiency, trypsin sensitivity, and optical properties of Arg96, Glu222, and Gly67 variants of green fluorescent protein

Sniegowski, Jennifer A.; Phail, Marlene E.; Wachter, Rebekka M.

doi:10.1016/j.bbrc.2005.04.166

Cited by 75 publications

(89 citation statements)

References 32 publications

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“…figure 1 also shows that in neither model the free or the total Bcd concentrations follow the mRNA distribution given by θ(z). This implies that, for our model, the Bcd concentration distribution is not a passive reflection of the mRNA that produces it, as assumed in [Spirov et al, 2009]. Comparing the values ofα and α used in figure 1 with previously reported ones, 0.0003s −1 − 0.0015s −1 [Grimm et al, 2010, Gregor et al, 2007a, Drocco et al, 2011, we observe that the one used in the total degradation model is within this previous estimated range, while the one used in the partial degradation model is larger.…”

Section: Reproduction Of the Gradientsupporting

confidence: 75%

“…Another model stated that the stability of the gradient between n.c. 10 and 14 could be explained in terms of an underlying mRNA gradient [Spirov et al, 2009]. The distribution of mRNA was measured in [Little et al, 2011] finding that it is bell-shaped with an 80% concentrated within the 20% of the total embryo's length that lies closest to the anterior pole.…”

Section: Introductionmentioning

confidence: 99%

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The effect of reactions on the formation and readout of the gradient of Bicoid

Ipiña

Dawson

2017

Phys. Biol.

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Abstract. During early development, the establishment of gradients of transcriptional factors determines the patterning of cell fates. The case of Bicoid (Bcd) in Drosophila melanogaster embryos is well documented and studied. There are still controversies as to whether SDD models in which Bcd is Synthesized at one end, then Diffuses and is Degraded can explain the gradient formation within the timescale observed experimentally. The Bcd gradient is observed in embryos that express a Bicoid-eGFP fusion protein (Bcd-GFP) which cannot differentiate if Bcd is freely diffusing or bound to immobile sites. In this work we analyze an SDID model that includes the Interaction of Bcd with binding sites. Using previously determined biophysical parameters we find that this model can explain the gradient formation within the experimentally observed time. Analyzing the differences between the free and bound Bcd distributions we observe that the latter spans over a longer lengthscale. We conclude that deriving the lengthscale from the distribution of Bcd-GFP can lead to an overestimation of the gradient lengthscale and of the degree of cooperativity that explains the distribution of the protein Hunchback whose production is regulated by Bcd.

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Section: Reproduction Of the Gradientsupporting

confidence: 75%

Section: Introductionmentioning

confidence: 99%

The effect of reactions on the formation and readout of the gradient of Bicoid

Ipiña

Dawson

2017

Phys. Biol.

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“…In this respect, FPs are relatively protease-sensitive prior to folding, whereas the compact nature of the barrel confers resistance to proteolytic digestion (35,54,55). mCherry RNCs with C-terminal tethers of 1, 15, 22, and 31 aa were all resistant to digestion at the lowest concentration (0.1 g/ml), whereas only polypeptides containing the 31-aa tether remained resistant at 10 g/ml (Fig.…”

Section: C-terminal Tether Length Influences Conformation Of Kineticamentioning

confidence: 98%

Kinetic Analysis of Ribosome-bound Fluorescent Proteins Reveals an Early, Stable, Cotranslational Folding Intermediate

Kelkar

Khushoo

Yang

et al. 2012

Journal of Biological Chemistry

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Background: Protein folding in cells is intimately coupled to protein synthesis. Results: GFP and RFP folding involves slow, cell autonomous insertion of the last ␤-strand into a stable cotranslational folding intermediate. Conclusion:Fluorescent ␤-barrel proteins utilize kinetically coupled co-and post-translational folding strategies. Significance: Specialized folding properties of GFP and RFP facilitate fluorescence acquisition in diverse biological environments.

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“…Considering the fact that any aromatic residue can replace Tyr66, it is curious that this amino acid is so highly conserved, but it may be necessary to ensure complete and successful maturation of the chromophore. Arg96 and Glu222 are catalytic residues positioned near the chromophore that are essential to the maturation process (Sniegowski et al 2005).…”

Section: Features Of a Victoria Gfpmentioning

confidence: 99%

Fluorescent Protein Tracking and Detection: Fluorescent Protein Structure and Color Variants

Rizzo¹,

Davidson²,

Piston³

2009

Cold Spring Harb Protoc

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INTRODUCTIONThe rapidly growing arsenal of genetically encoded fluorescent proteins (FPs) obtained from sea creatures has launched and fueled a revolution in live cell imaging. The diverse array of applications benefiting from FPs ranges from markers targeted at organelles and protein fusions designed to monitor intracellular dynamics to reporters of transcriptional regulation and in vivo probes for whole-body imaging and detection of cancer. FPs have enabled the creation of highly specific biosensors to monitor a wide range of intracellular phenomena, including pH and metal-ion concentration, protein kinase activity, apoptosis, membrane voltage, cyclic nucleotide signaling, and tracing neuronal pathways. The purpose of this article is to provide a description of the wide variety of FPs that are currently available.

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Maturation efficiency, trypsin sensitivity, and optical properties of Arg96, Glu222, and Gly67 variants of green fluorescent protein

Cited by 75 publications

References 32 publications

The effect of reactions on the formation and readout of the gradient of Bicoid

The effect of reactions on the formation and readout of the gradient of Bicoid

Kinetic Analysis of Ribosome-bound Fluorescent Proteins Reveals an Early, Stable, Cotranslational Folding Intermediate

Fluorescent Protein Tracking and Detection: Fluorescent Protein Structure and Color Variants

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