scholarly journals Fluorescent protein‐mediated colour polymorphism in reef corals: multicopy genes extend the adaptation/acclimatization potential to variable light environments

2015 ◽  
Vol 24 (2) ◽  
pp. 453-465 ◽  
Author(s):  
John R. Gittins ◽  
Cecilia D'Angelo ◽  
Franz Oswald ◽  
Richard J. Edwards ◽  
Jörg Wiedenmann
Keyword(s):  
Fluorescent Protein ◽  
Colour Polymorphism ◽  
Reef Corals ◽  
Variable Light ◽  
Multicopy Genes

scholarly journals Fluorescence color diversity of great barrier reef corals

2015 ◽  
Vol 08 (04) ◽  
pp. 1550028 ◽  
Author(s):  
Grigory Lapshin ◽  
Anya Salih ◽  
Peter Kolosov ◽  
Maria Golovkina ◽  
Yuri Zavorotnyi ◽  
...  
Keyword(s):  
Great Barrier Reef ◽  
Fluorescent Protein ◽  
Laser Fluorescence ◽  
Barrier Reef ◽  
Post Translational Modification ◽  
Post Translational Modifications ◽  
Reef Corals ◽  
Fluorescence Color ◽  
Fluorescent Spectra ◽  
Green Fluorescent

A group of variously colored proteins belonging to the green fluorescent protein (GFP) family are responsible for coloring coral tissues. Corals of the Great Barrier Reef were studied with the custom-built fiber laser fluorescence spectrometers. Spectral analysis showed that most of the examined corals contained multiple fluorescent peaks ranging from 470 to 620 nm. This observation was attributed to the presence of multiple genes of GFP-like proteins in a single coral, as well as by the photo-induced post-translational modifications of certain GFP-like proteins. We isolated a novel photo-convertible fluorescent protein (FP) from one of the tested corals. We propose that two processes may explain the observed diversity of the fluorescent spectra in corals: (1) dark post-translational modification (maturation), and (2) color photo-conversion of certain maturated proteins in response to sunlight.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

First record of body colour polymorphism in giant African snail Achatina fulica (Bowdich, 1822) - a comparative study using mitochondrial cytochrome oxidase subunit I (COI) gene

ENTOMON ◽  
2019 ◽  
Vol 44 (2) ◽  
pp. 155-160
Author(s):  
Keerthy Vijayan ◽  
R. Sugantha Sakthivel ◽  
T.V. Sajeev
Keyword(s):  
Cytochrome Oxidase ◽  
South India ◽  
The Body ◽  
Colour Polymorphism ◽  
Coi Gene ◽  
Body Colour ◽  
Cytochrome Oxidase Subunit ◽  
Cytochrome Oxidase Subunit I ◽  
Black And White ◽  
Oxidase Subunit

The presence of the body colour polymorphism in the tropical invasive pest giant African snail is reported for the first time from South India. Three different body colour polymorphs were recognised viz. grey, black and white. The grey body colour is the most common polymorph. The black and white colour polymorphs are found to be in almost equal proportions in the reported localities with the grey counterparts. The cytochrome oxidase subunit I (COI) sequences of the three colour polymorphs are found to be identical. The presence of the body colour polymorphism in south India may be attributed to the avian predation and other selection pressures.

Effects of tropical storms on the demography of reef corals

2018 ◽  
Vol 606 ◽  
pp. 29-38 ◽  
Author(s):  
AH Baird ◽  
M Álvarez-Noriega ◽  
VR Cumbo ◽  
SR Connolly ◽  
M Dornelas ◽  
...  
Keyword(s):  
Tropical Storms ◽  
Reef Corals

A high-throughput yellow fluorescent protein (YFP) cell-based screen identifies autophagy modulators to increase the effectiveness of radioiodine therapy

2019 ◽  
Author(s):  
Martin Read ◽  
Katie Baker ◽  
Alice Fletcher ◽  
Caitlin Thornton ◽  
Mohammed Alshahrani ◽  
...  
Keyword(s):  
High Throughput ◽  
Fluorescent Protein ◽  
Radioiodine Therapy ◽  
Yellow Fluorescent Protein

A Unified Model for Photophysical and Electro-Optical Properties of Green Fluorescent Proteins

2019 ◽  
Author(s):  
Chi-Yun Lin ◽  
Matthew Romei ◽  
Luke Oltrogge ◽  
Irimpan Mathews ◽  
Steven Boxer
Keyword(s):  
Driving Force ◽  
Fluorescent Protein ◽  
Charge Transfer Band ◽  
Photophysical Properties ◽  
Polymethine Dyes ◽  
Emission Rates ◽  
Unified Framework ◽  
Underlying Factor ◽  
Green Fluorescent ◽  
Protein Environment

Green fluorescent protein (GFPs) have become indispensable imaging and optogenetic tools. Their absorption and emission properties can be optimized for specific applications. Currently, no unified framework exists to comprehensively describe these photophysical properties, namely the absorption maxima, emission maxima, Stokes shifts, vibronic progressions, extinction coefficients, Stark tuning rates, and spontaneous emission rates, especially one that includes the effects of the protein environment. In this work, we study the correlations among these properties from systematically tuned GFP environmental mutants and chromophore variants. Correlation plots reveal monotonic trends, suggesting all these properties are governed by one underlying factor dependent on the chromophore's environment. By treating the anionic GFP chromophore as a mixed-valence compound existing as a superposition of two resonance forms, we argue that this underlying factor is defined as the difference in energy between the two forms, or the driving force, which is tuned by the environment. We then introduce a Marcus-Hush model with the bond length alternation vibrational mode, treating the GFP absorption band as an intervalence charge transfer band. This model explains all the observed strong correlations among photophysical properties; related subtopics are extensively discussed in Supporting Information. Finally, we demonstrate the model's predictive power by utilizing the additivity of the driving force. The model described here elucidates the role of the protein environment in modulating photophysical properties of the chromophore, providing insights and limitations for designing new GFPs with desired phenotypes. We argue this model should also be generally applicable to both biological and non-biological polymethine dyes.<br>

Site-Specific Protein Covalent Attachment to Nanotubes and Its Electronic Impact on Single Molecule Function

2019 ◽  
Author(s):  
Adam Beachey ◽  
Harley Worthy ◽  
William David Jamieson ◽  
Suzanne Thomas ◽  
Benjamin Bowen ◽  
...  
Keyword(s):  
Single Molecule ◽  
Fluorescent Protein ◽  
Functional Integration ◽  
Attachment Site ◽  
Covalent Attachment ◽  
Great Promise ◽  
Functional Coupling ◽  
Phenyl Azide ◽  
Electronic Impact ◽  
Protein Attachment

<p>Functional integration of proteins with carbon-based nanomaterials such as nanotubes holds great promise in emerging electronic and optoelectronic applications. Control over protein attachment poses a major challenge for consistent and useful device fabrication, especially when utilizing single/few molecule properties. Here, we exploit genetically encoded phenyl azide photochemistry to define the direct covalent attachment of three different proteins, including the fluorescent protein GFP, to carbon nanotube side walls. Single molecule fluorescence revealed that on attachment to SWCNTs GFP’s fluorescence changed in terms of intensity and improved resistance to photobleaching; essentially GFP is fluorescent for much longer on attachment. The site of attachment proved important in terms of electronic impact on GFP function, with the attachment site furthest from the functional center having the larger effect on fluorescence. Our approach provides a versatile and general method for generating intimate protein-CNT hybrid bioconjugates. It can be potentially applied easily to any protein of choice; attachment position and thus interface characteristics with the CNT can easily be changed by simply placing the phenyl azide chemistry at different residues by gene mutagenesis. Thus, our approach will allow consistent construction and modulate functional coupling through changing the protein attachment position.</p>

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