Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.

Light is an important environmental factor for almost all organisms. It is mainly used as an energy source but it is also a key factor for the regulation of multiple cellular functions. Light as the extracellular stimulus is thereby converted into an intracellular signal by photoreceptors that act a...

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Main Authors: Matthias Dorn, Marcel Jurk, Peter Schmieder
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3256143?pdf=render
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author Matthias Dorn
Marcel Jurk
Peter Schmieder
author_facet Matthias Dorn
Marcel Jurk
Peter Schmieder
author_sort Matthias Dorn
collection DOAJ
description Light is an important environmental factor for almost all organisms. It is mainly used as an energy source but it is also a key factor for the regulation of multiple cellular functions. Light as the extracellular stimulus is thereby converted into an intracellular signal by photoreceptors that act as signal transducers. The blue-light receptor YtvA, a bacterial counterpart of plant phototropins, is involved in the stress response of Bacillus subtilis. The mechanism behind its activation, however, remains unknown. It was suggested based on fluorescence spectroscopic studies that YtvA function involves GTP binding and that this interaction is altered by absorption of light. We have investigated this interaction by several biophysical methods and show here using fluorescence spectroscopy, ITC titrations, and three NMR spectroscopic assays that while YtvA interacts with BODIPY-GTP as a fluorescent GTP analogue originally used for the detection of GTP binding, it does not bind GTP.
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spelling doaj.art-5c18c929139b421c952a4f92949832512022-12-22T03:42:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0171e2920110.1371/journal.pone.0029201Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.Matthias DornMarcel JurkPeter SchmiederLight is an important environmental factor for almost all organisms. It is mainly used as an energy source but it is also a key factor for the regulation of multiple cellular functions. Light as the extracellular stimulus is thereby converted into an intracellular signal by photoreceptors that act as signal transducers. The blue-light receptor YtvA, a bacterial counterpart of plant phototropins, is involved in the stress response of Bacillus subtilis. The mechanism behind its activation, however, remains unknown. It was suggested based on fluorescence spectroscopic studies that YtvA function involves GTP binding and that this interaction is altered by absorption of light. We have investigated this interaction by several biophysical methods and show here using fluorescence spectroscopy, ITC titrations, and three NMR spectroscopic assays that while YtvA interacts with BODIPY-GTP as a fluorescent GTP analogue originally used for the detection of GTP binding, it does not bind GTP.http://europepmc.org/articles/PMC3256143?pdf=render
spellingShingle Matthias Dorn
Marcel Jurk
Peter Schmieder
Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.
PLoS ONE
title Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.
title_full Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.
title_fullStr Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.
title_full_unstemmed Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.
title_short Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not.
title_sort blue news update bodipy gtp binds to the blue light receptor ytva while gtp does not
url http://europepmc.org/articles/PMC3256143?pdf=render
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