The University of Southampton
University of Southampton Institutional Repository

It's cheap to be colorful: anthozoans show a slow turnover of GFP-like proteins

It's cheap to be colorful: anthozoans show a slow turnover of GFP-like proteins
It's cheap to be colorful: anthozoans show a slow turnover of GFP-like proteins
Pigments homologous to the green fluorescent protein (GFP) contribute up to 14% of the soluble protein content of many anthozoans. Maintenance of such high tissue levels poses a severe energetic penalty to the animals if protein turnover is fast. To address this as yet unexplored issue, we established that the irreversible green-to-red conversion of the GFP-like pigments from the reef corals Montastrea cavernosa (mcavRFP) and Lobophyllia hemprichii (EosFP) is driven by violet–blue radiation in vivo and in situ. In the absence of photoconverting light, we subsequently tracked degradation of the red-converted forms of the two proteins in coral tissue using in vivo spectroscopy and immunochemical detection of the post-translational peptide backbone modification. The pigments displayed surprisingly slow decay rates, characterized by half-lives of 20 days. The slow turnover of GFP-like proteins implies that the associated energetic costs for being colorful are comparatively low. Moreover, high in vivo stability makes GFP-like proteins suitable for functions requiring high pigment concentrations, such as photoprotection.
coral pigments, green fluorescent protein, photoconversion, protein half-life, protein metabolism
1742-464X
2496-2505
Leutenegger, Alexandra
a0118282-9639-408e-8379-295665553caf
D'Angelo, Cecilia
0d35b03b-684d-43aa-a57a-87212ab07ee1
Matz, Mikhail V.
9a128396-eaf1-4c49-aac4-aa160d01e393
Denzel, Andrea
41266ff8-cbf4-4195-96ab-07824ec50838
Oswald, Franz
a5b02f2d-8439-411b-b5ad-999629cee58f
Salih, Anya
fb71f3bf-e1aa-4b78-a2c6-7ab5eaf4bdd4
Ulrich Nienhaus, G.
a3b9e10a-d2b2-487d-a094-15c2895724b2
Wiedenmann, Jörg
ad445af2-680f-4927-90b3-589ac9d538f7
Leutenegger, Alexandra
a0118282-9639-408e-8379-295665553caf
D'Angelo, Cecilia
0d35b03b-684d-43aa-a57a-87212ab07ee1
Matz, Mikhail V.
9a128396-eaf1-4c49-aac4-aa160d01e393
Denzel, Andrea
41266ff8-cbf4-4195-96ab-07824ec50838
Oswald, Franz
a5b02f2d-8439-411b-b5ad-999629cee58f
Salih, Anya
fb71f3bf-e1aa-4b78-a2c6-7ab5eaf4bdd4
Ulrich Nienhaus, G.
a3b9e10a-d2b2-487d-a094-15c2895724b2
Wiedenmann, Jörg
ad445af2-680f-4927-90b3-589ac9d538f7

Leutenegger, Alexandra, D'Angelo, Cecilia, Matz, Mikhail V., Denzel, Andrea, Oswald, Franz, Salih, Anya, Ulrich Nienhaus, G. and Wiedenmann, Jörg (2007) It's cheap to be colorful: anthozoans show a slow turnover of GFP-like proteins. Febs Journal, 274 (10), 2496-2505. (doi:10.1111/j.1742-4658.2007.05785.x). (PMID:17419724)

Record type: Article

Abstract

Pigments homologous to the green fluorescent protein (GFP) contribute up to 14% of the soluble protein content of many anthozoans. Maintenance of such high tissue levels poses a severe energetic penalty to the animals if protein turnover is fast. To address this as yet unexplored issue, we established that the irreversible green-to-red conversion of the GFP-like pigments from the reef corals Montastrea cavernosa (mcavRFP) and Lobophyllia hemprichii (EosFP) is driven by violet–blue radiation in vivo and in situ. In the absence of photoconverting light, we subsequently tracked degradation of the red-converted forms of the two proteins in coral tissue using in vivo spectroscopy and immunochemical detection of the post-translational peptide backbone modification. The pigments displayed surprisingly slow decay rates, characterized by half-lives of 20 days. The slow turnover of GFP-like proteins implies that the associated energetic costs for being colorful are comparatively low. Moreover, high in vivo stability makes GFP-like proteins suitable for functions requiring high pigment concentrations, such as photoprotection.

This record has no associated files available for download.

More information

Published date: May 2007
Keywords: coral pigments, green fluorescent protein, photoconversion, protein half-life, protein metabolism
Organisations: Ocean and Earth Science

Identifiers

Local EPrints ID: 48215
URI: http://eprints.soton.ac.uk/id/eprint/48215
ISSN: 1742-464X
PURE UUID: 98486147-12cf-4e55-92db-a15490d6a934
ORCID for Jörg Wiedenmann: ORCID iD orcid.org/0000-0003-2128-2943

Catalogue record

Date deposited: 07 Sep 2007
Last modified: 16 Mar 2024 03:53

Export record

Altmetrics

Contributors

Author: Alexandra Leutenegger
Author: Mikhail V. Matz
Author: Andrea Denzel
Author: Franz Oswald
Author: Anya Salih
Author: G. Ulrich Nienhaus

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×