Surface views of the CSL coactivator complex (upper) and corepressor complexes (lower).

<p>(A) The DNA-bound CSL activator complex consists of CSL (green), NICD (RAM domain, red; ankyrin repeats, yellow), and mastermind (MAM, orange). (PDB-ID: 1TTU). (B) KyoT2 (red) interacts with the BTD of CSL, similar to the NICD RAM domain (RAM-type). (PDB-ID: 4J2X). (C) Hairless interacts with the CTD of Su(H), resulting in a dramatic change of CTD conformation (H-type). (PDB-ID: 5E24). (D) The crystal structure of the SMRT/HDAC1 associated repressor protein (SHARP)-CSL corepressor complex and the CSL-RBPJ interacting and tubulin associated (RITA) corepressor complex is unknown at the moment (PDB-ID, RBPJ bound to DNA: 3BRG).</p

Available CSL complex structure data (protein data bank [PDB] database).

<p>Available CSL complex structure data (protein data bank [PDB] database).</p

amilFP597 exon 3 sequences

The chromophore coding sequences of RFP-related genes of A. millepora were amplified using genomic DNA of LR, MR and HR morphs as the template with primers designed to conserved regions within exon 3

amilFP597 promoter

Analysis of the amilFP597 promoter copy ratios in six A. millepora morphs with different levels of redness

Spectroscopic characteristics of GFP-like proteins

All spectroscopic data utilised for the characterisation of amilFP597, amilCP506, amilCP564 and amilFP60

amilFP597 copies

Copy numbers of amilFP597 variant genes determined by semi-quantitative PCR amplification of a conserved genomic exon 3 fragment and by diagnostic restriction analysis with ApeK1

Sequences RFP full length genes

All raw sequences used to reconstruct the amilFP597 gene in A. millepora.Full-length sequences of indel (-) and indel (+) promoter variants of the amilFP597 gene were obtained for the MR morph. These sequences, extending from the promoter region to the 3’UTR, were produced by joining the sequences of two overlapping PCR products covering the 5’ region [promoter to exon 3 amplified using primers pRFPlargeF (+) or pRFPsmallF (-) and RFP SP1] and the 3’ region (intron 2 to 3’UTR amplified using primers RFP_I2-3’U_F and RFP_I2-3’U_R2). Sequence differences in the overlap between the 5’ and 3’ region fragments were used to assign the latter to either the indel (+) or indel (-) promoter variant genes. The promoter-exon 3 and intron 2-3’UTR fragments were cloned and sequenced on both strands using vector primers and by primer walking. The assembled sequences have been submitted to GenBank as accessions KC818413 [indel (-) gene] and KC818414 [indel (+) gene]

Abs spectra of A millepora

Absorption spectra of clarified tissue extracts of the HR and LR A. millepora morphs. The absorption spectrum of purified recombinant amilFP597 normalised to the peak value of the HR spectrum is included for comparison

Photoswitching of the chromophore in cerFP505.

<p>A) Absorption spectra after irradiation with 400 nm (on-state) or with 450 nm light (off-state). Deactivation gives rise to a second peak around 390 nm. B) Ground state equilibrium. Irradiation at 400 nm drives the protein to the on-state, 450 nm light turns off the “activatable” fraction of the protein. Bars above the x-axis specify the light treatment, 400 nm light (white bar), 450 nm light (grey bar) or no light (black bar). C) Fluorescence emission of the protein in the on- or off-state was recorded for ≥30 min in the dark after 5 min irradiation with 400 or 450 nm light. Bars above the x-axis specify the light treatment as described above. D) The reversibility of the reaction is shown for eight cycles of activation/deactivation. Bars above the x-axis specify the light treatment as described in (B).</p

Identification of a GFP-like protein from a deep sea ceriantharian.

<p>A) Fluorescence image of a ceriantharian acquired in 530 m depth in the Gulf of Mexico. The depth (ft), temperature (Temp, °C) and the salinity (Salin) measured during image acquisition are displayed in the upper part of the panel. B–C) Microscopic image of two tentacles photographed under white light (B) or blue light excitation using a GFP-filter set (C). D) Absorption, excitation and emission spectra of purified recombinant cerFP505. Fluorescence spectra were recorded using 450 nm light for excitation, whereas the emission was collected at 550 nm. E) Multiple alignment of amino acid sequences from ceriantharian fluorescent proteins and EGFP. The chromophore – forming tripeptide is highlighted in green. Residues interacting directly with, or found in the proximity of, the chromophore in cmFP512 are labeled in blue or red, respectively. Amino acids underlayed in grey or yellow are involved in A/B or A/C interface interactions in cmFP512, respectively <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0003766#pone.0003766-Nienhaus1" target="_blank">[59]</a>. The numberings for cerFP505 and EGFP are given above and below the sequences, respectively. Regions forming ß-sheets in EGFP are underlined.</p