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Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP.
Proc Natl Acad Sci U S A. 2005 Jun 28; 102(26):9156-9.PN

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 approximately 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.

Authors+Show Affiliations

Department of Biophysics and General Zoology, University of Ulm, Albert-Einstein-Allee 11, D-89081 Ulm, Germany.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15964985

Citation

Nienhaus, Karin, et al. "Structural Basis for Photo-induced Protein Cleavage and Green-to-red Conversion of Fluorescent Protein EosFP." Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 26, 2005, pp. 9156-9.
Nienhaus K, Nienhaus GU, Wiedenmann J, et al. Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP. Proc Natl Acad Sci USA. 2005;102(26):9156-9.
Nienhaus, K., Nienhaus, G. U., Wiedenmann, J., & 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 of the United States of America, 102(26), 9156-9.
Nienhaus K, et al. Structural Basis for Photo-induced Protein Cleavage and Green-to-red Conversion of Fluorescent Protein EosFP. Proc Natl Acad Sci USA. 2005 Jun 28;102(26):9156-9. PubMed PMID: 15964985.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP. AU - Nienhaus,Karin, AU - Nienhaus,G Ulrich, AU - Wiedenmann,Jörg, AU - Nar,Herbert, Y1 - 2005/06/17/ PY - 2005/6/21/pubmed PY - 2005/8/12/medline PY - 2005/6/21/entrez SP - 9156 EP - 9 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc. Natl. Acad. Sci. U.S.A. VL - 102 IS - 26 N2 - 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 approximately 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. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/15964985/Structural_basis_for_photo_induced_protein_cleavage_and_green_to_red_conversion_of_fluorescent_protein_EosFP_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=15964985 DB - PRIME DP - Unbound Medicine ER -