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      • Abstract: found
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      Ultramarine, a Chromoprotein Acceptor for Förster Resonance Energy Transfer

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          Abstract

          We have engineered a monomeric blue non-fluorescent chromoprotein called Ultramarine (fluorescence quantum yield, 0.001; ε 585 nm, 64,000 M −1. cm −1) for use as a Förster resonance energy transfer acceptor for a number of different donor fluorescent proteins. We show its use for monitoring activation of caspase 3 in live cells using fluorescence lifetime imaging. Ultramarine has the potential to increase the number of cellular parameters that can be imaged simultaneously.

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          Cell death: critical control points.

          Nika Danial, Stanley Korsmeyer (2004)
          Programmed cell death is a distinct genetic and biochemical pathway essential to metazoans. An intact death pathway is required for successful embryonic development and the maintenance of normal tissue homeostasis. Apoptosis has proven to be tightly interwoven with other essential cell pathways. The identification of critical control points in the cell death pathway has yielded fundamental insights for basic biology, as well as provided rational targets for new therapeutics.
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            Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae.

            Mark A Sheff, Kurt S. Thorn (2004)
            Green fluorescent protein (GFP) has become an increasingly popular protein tag for determining protein localization and abundance. With the availability of GFP variants with altered fluorescence spectra, as well as GFP homologues from other organisms, multi-colour fluorescence with protein tags is now possible, as is measuring protein interactions using fluorescence resonance energy transfer (FRET). We have created a set of yeast tagging vectors containing codon-optimized variants of GFP, CFP (cyan), YFP (yellow), and Sapphire (a UV-excitable GFP). These codon-optimized tags are twice as detectable as unoptimized tags. We have also created a tagging vector containing the monomeric DsRed construct tdimer2, which is up to 15-fold more detectable than tags currently in use. These tags significantly improve the detection limits for live-cell fluorescence imaging in yeast, and provide sufficient distinguishable fluorophores for four-colour imaging. Copyright 2004 John Wiley & Sons, Ltd.
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              Creating new fluorescent probes for cell biology.

              Jin. Zhang, Robert E. Campbell, Alice Ting … (2002)
              Fluorescent probes are one of the cornerstones of real-time imaging of live cells and a powerful tool for cell biologists. They provide high sensitivity and great versatility while minimally perturbing the cell under investigation. Genetically-encoded reporter constructs that are derived from fluorescent proteins are leading a revolution in the real-time visualization and tracking of various cellular events. Recent advances include the continued development of 'passive' markers for the measurement of biomolecule expression and localization in live cells, and 'active' indicators for monitoring more complex cellular processes such as small-molecule-messenger dynamics, enzyme activation and protein-protein interactions.
              Article 0 comments Cited 283 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                : Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (iso-abbrev): PLoS ONE
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2012
                Publication date (Electronic): 16 July 2012
                Volume: 7
                Issue: 7
                Electronic Location Identifier: e41028
                Affiliations
                [1 ]Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Victoria, Australia
                [2 ]ARC Centre of Excellence for Structural and Functional Microbial Genomics, Monash University, Clayton Campus, Victoria, Australia
                [3 ]Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia
                Stanford, United States of America
                Author notes

                Conceived and designed the experiments: AP MP. Performed the experiments: AP M. Prescott LG M. Perugini. Analyzed the data: AP M. Prescott M. Perugini. Contributed reagents/materials/analysis tools: M. Perugini. Wrote the paper: AP M. Prescott RJD.

                [¤]

                Current address: The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia

                Article
                Publisher ID: PONE-D-12-05383
                DOI: 10.1371/journal.pone.0041028
                PMC ID: 3397996
                PubMed ID: 22815901
                SO-VID: 345ce73e-1b2a-442b-8579-c2b9debb4067
                Copyright © Pettikiriarachchi et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                Date received : 15 February 2012
                Date accepted : 17 June 2012
                Page count
                Pages: 9
                Categories
                Subject: Research Article
                Subject: Biology
                Subject: Biochemistry
                Subject: Proteins
                Subject: Chromoproteins
                Subject: Luminescent Proteins
                Subject: Protein Chemistry
                Subject: Protein Interactions
                Subject: Recombinant Proteins
                Subject: Biophysics
                Subject: Protein Chemistry
                Subject: Molecular Cell Biology
                Subject: Physics
                Subject: Biophysics
                Subject: Protein Chemistry

                ScienceOpen disciplines: Uncategorized
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                ScienceOpen disciplines: Uncategorized

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