Evidence map›Paper›PMID 26561348›Full record

ArticlePloS one2015

Adaptive Evolution of Eel Fluorescent Proteins from Fatty Acid Binding Proteins Produces Bright Fluorescence in the Marine Environment.

David F Gruber, Jean P Gaffney, Shaadi Mehr, Rob DeSalle, John S Sparks, Jelena Platisa, Vincent A Pieribone

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

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  13. Naturally occurring fluorescence in frogs.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

David F GruberBaruch College, Department of Natural Sciences, City University of New York, New York, New York, United States of America.
Jean P GaffneyBaruch College, Department of Natural Sciences, City University of New York, New York, New York, United States of America.
Shaadi MehrState University of New York, Biological Science Department, College at Old Westbury, Old Westbury, New York, United States of America.
Rob DeSalleAmerican Museum of Natural History, Sackler Institute for Comparative Genomics,Central Park W at 79th St, New York, New York, United States of America.
John S SparksAmerican Museum of Natural History, Sackler Institute for Comparative Genomics,Central Park W at 79th St, New York, New York, United States of America.
Jelena PlatisaThe John B. Pierce Laboratory, Inc., New Haven, Connecticut, United States of America.
Vincent A PieriboneThe John B. Pierce Laboratory, Inc., New Haven, Connecticut, United States of America.

Funding

Genetically-Encoded Voltage Probe DevelopmentR01NS083875 · NINDS · JOHN B. PIERCE LABORATORY, INC. · PI HUGHES, THOMAS E, NITABACH, MICHAEL · 2013 to 2016
$2.3M
Development of Protein-based Voltage ProbesU01NS090565 · NINDS · JOHN B. PIERCE LABORATORY, INC. · PI PIERIBONE, VINCENT A · 2014 to 2016
$1.7M
NINDS NIH HHS R01 NS083875NINDS NIH HHS R01NS083875NINDS NIH HHS U01 NS090565NINDS NIH HHS U01NS090565-02
6 · The paper itself

Abstract

We report the identification and characterization of two new members of a family of bilirubin-inducible fluorescent proteins (FPs) from marine chlopsid eels and demonstrate a key region of the sequence that serves as an evolutionary switch from non-fluorescent to fluorescent fatty acid-binding proteins (FABPs). Using transcriptomic analysis of two species of brightly fluorescent Kaupichthys eels (Kaupichthys hyoproroides and Kaupichthys n. sp.), two new FPs were identified, cloned and characterized (Chlopsid FP I and Chlopsid FP II). We then performed phylogenetic analysis on 210 FABPs, spanning 16 vertebrate orders, and including 163 vertebrate taxa. We show that the fluorescent FPs diverged as a protein family and are the sister group to brain FABPs. Our results indicate that the evolution of this family involved at least three gene duplication events. We show that fluorescent FABPs possess a unique, conserved tripeptide Gly-Pro-Pro sequence motif, which is not found in non-fluorescent fatty acid binding proteins. This motif arose from a duplication event of the FABP brain isoforms and was under strong purifying selection, leading to the classification of this new FP family. Residues adjacent to the motif are under strong positive selection, suggesting a further refinement of the eel protein's fluorescent properties. We present a phylogenetic reconstruction of this emerging FP family and describe additional fluorescent FABP members from groups of distantly related eels. The elucidation of this class of fish FPs with diverse properties provides new templates for the development of protein-based fluorescent tools. The evolutionary adaptation from fatty acid-binding proteins to fluorescent fatty acid-binding proteins raises intrigue as to the functional role of bright green fluorescence in this cryptic genus of reclusive eels that inhabit a blue, nearly monochromatic, marine environment.

Indexed as

Adaptation, PhysiologicalBiological EvolutionMarine BiologyAmino Acid SequenceAnimalsEelsFatty Acid-Binding ProteinsHEK293 CellsHumansLuminescent ProteinsMolecular Sequence DataPhylogenySequence Homology, Amino AcidFatty Acid-Binding ProteinsLuminescent Proteins

Identifiers

PMID26561348
PMCPMC4641735

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.