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Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP

Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP
Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP
Genetically encoded fusion constructs derived from fluorescent proteins (FPs) can be designed to report on a multitude of events and signals in cells, tissues, and entire organs without interfering with the complex machinery of life. EosFP is a novel FP from the scleractinian coral Lobophyllia hemprichii that switches its fluorescence emission from green (516 nm) to red (581 nm) upon irradiation with 400-nm light. This property enables localized tagging of proteins and thus provides a valuable tool for tracking protein movements within live cells. Here, we present the x-ray structures of the green and red forms of WT EosFP. They reveal that formation of the red chromophore is associated with cleavage of the peptide backbone, with surprisingly little change elsewhere in the structure, and provide insights into the mechanism that generates this interesting posttranslational polypeptide modification.
photochemistry, photoconversion, x-ray structure, Anthozoa
0027-8424
9156-9159
Nienhaus, K.
ff9b0d42-5cd8-49a7-8ed4-24db20289091
Nienhaus, G.U.
8f2b40ea-be57-4b32-880f-8a0e5c1585aa
Wiedenmann, J.
ad445af2-680f-4927-90b3-589ac9d538f7
Nar, H.
e43686d6-f635-4a73-ab8e-a2d140e79e4b
Nienhaus, K.
ff9b0d42-5cd8-49a7-8ed4-24db20289091
Nienhaus, G.U.
8f2b40ea-be57-4b32-880f-8a0e5c1585aa
Wiedenmann, J.
ad445af2-680f-4927-90b3-589ac9d538f7
Nar, H.
e43686d6-f635-4a73-ab8e-a2d140e79e4b

Nienhaus, K., Nienhaus, G.U., Wiedenmann, J. and Nar, H. (2005) Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP. Proceedings of the National Academy of Sciences, 102 (26), 9156-9159. (doi:10.1073/pnas.0501874102).

Record type: Article

Abstract

Genetically encoded fusion constructs derived from fluorescent proteins (FPs) can be designed to report on a multitude of events and signals in cells, tissues, and entire organs without interfering with the complex machinery of life. EosFP is a novel FP from the scleractinian coral Lobophyllia hemprichii that switches its fluorescence emission from green (516 nm) to red (581 nm) upon irradiation with 400-nm light. This property enables localized tagging of proteins and thus provides a valuable tool for tracking protein movements within live cells. Here, we present the x-ray structures of the green and red forms of WT EosFP. They reveal that formation of the red chromophore is associated with cleavage of the peptide backbone, with surprisingly little change elsewhere in the structure, and provide insights into the mechanism that generates this interesting posttranslational polypeptide modification.

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More information

Published date: 28 June 2005
Keywords: photochemistry, photoconversion, x-ray structure, Anthozoa
Organisations: Ocean and Earth Science

Identifiers

Local EPrints ID: 51184
URI: https://eprints.soton.ac.uk/id/eprint/51184
ISSN: 0027-8424
PURE UUID: fb95075b-9c22-433e-b18d-bf717f59f3d5
ORCID for J. Wiedenmann: ORCID iD orcid.org/0000-0003-2128-2943

Catalogue record

Date deposited: 08 May 2008
Last modified: 14 Mar 2019 01:40

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