Evidence map›Paper›PMID 16299587›Full record

ArticlePLoS genetics2005

Drosophila tan encodes a novel hydrolase required in pigmentation and vision.

John R True, Shu-Dan Yeh, Bernhard T Hovemann, Tobias Kemme, Ian A Meinertzhagen, Tara N Edwards, Shian-Ren Liou, Qian Han, Jianyong Li

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

93 citing papers in PubMed, 187 citations in OpenAlex.

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  17. Science advances · 2022
    Article
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33 more citing papers are in PubMed but not listed here.

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

9 authors at 5 institutions in 3 countries.

John R TrueDepartment of Ecology and Evolution, State University of New York, Stony Brook, New York, United States of America. jrtrue@life.bio.sunysb.edu
Shu-Dan Yeh
Bernhard T Hovemann
Tobias Kemme
Ian A Meinertzhagen
Tara N Edwards
Shian-Ren Liou
Qian Han
Jianyong Li
Dalhousie University · CARuhr University Bochum · DEState University of New York · USUniversity of Illinois Urbana-Champaign · USStony Brook University · US

Funding

Biochemistry of Chorion Hardening in MosquitoesR01AI037789 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI LI, JIANYONG · 2001 to 2005
$1.3M
BIOCHEMISTRY OF EGG CHORION TANNING IN MOSQUITOESR29AI037789 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI LI, JIANYONG · 1995 to 1999
–
NIAID NIH HHS AI 37789NIAID NIH HHS R01 AI037789NIAID NIH HHS R29 AI037789
6 · The paper itself

Abstract

Many proteins are used repeatedly in development, but usually the function of the protein is similar in the different contexts. Here we report that the classical Drosophila melanogaster locus tan encodes a novel enzyme required for two very different cellular functions: hydrolysis of N-beta-alanyl dopamine (NBAD) to dopamine during cuticular melanization, and hydrolysis of carcinine to histamine in the metabolism of photoreceptor neurotransmitter. We characterized two tan-like P-element insertions that failed to complement classical tan mutations. Both are inserted in the 5' untranslated region of the previously uncharacterized gene CG12120, a putative homolog of fungal isopenicillin-N N-acyltransferase (EC 2.3.1.164). Both P insertions showed abnormally low transcription of the CG12120 mRNA. Ectopic CG12120 expression rescued tan mutant pigmentation phenotypes and caused the production of striking black melanin patterns. Electroretinogram and head histamine assays indicated that CG12120 is required for hydrolysis of carcinine to histamine, which is required for histaminergic neurotransmission. Recombinant CG12120 protein efficiently hydrolyzed both NBAD to dopamine and carcinine to histamine. We conclude that D. melanogaster CG12120 corresponds to tan. This is, to our knowledge, the first molecular genetic characterization of NBAD hydrolase and carcinine hydrolase activity in any organism and is central to the understanding of pigmentation and photoreceptor function.

Indexed as

Amino Acid SequenceAnimalsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDrosophilaDrosophila ProteinsElectroretinographyGene Expression Regulation, DevelopmentalGenetic Complementation TestMolecular Sequence DataMutationPigmentationSequence Homology, Amino AcidVision, OcularChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDrosophila Proteinst protein, Drosophila

Identifiers

PMID16299587
PMCPMC1285064
OpenAlexW2026199073

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.