Evidence map›Paper›PMID 26679720›Full record

ArticleScientific reports2015

Minimal domain of bacterial phytochrome required for chromophore binding and fluorescence.

Konstantin A Rumyantsev, Daria M Shcherbakova, Natalia I Zakharova, Alexander V Emelyanov, Konstantin K Turoverov, Vladislav V Verkhusha

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
12.4field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 55 citations in OpenAlex.

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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

6 authors at 3 institutions in 3 countries.

Konstantin A RumyantsevDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Daria M ShcherbakovaDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Natalia I ZakharovaDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Alexander V EmelyanovDepartment of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Konstantin K TuroverovLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg 194064, Russia.
Vladislav V VerkhushaDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Albert Einstein College of Medicine · USInstitute of Cytology · RUPeter the Great St. Petersburg Polytechnic University · RU

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
In Vivo Multiphoton Based Imaging of Complex Cancer Cell BehaviorR01CA164468 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2011 to 2015
$3.8M
Molecular Fluorescent ToolkitR01GM073913 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2006 to 2014
$2.4M
Technologies to Define and Map Novel Interorganelle Macromolecular InteractionsR01GM105997 · NIGMS · UNIVERSITY OF COLORADO · PI AHN, NATALIE G., PALMER, AMY E · 2013 to 2016
$1.6M
Engineering bacterial phytochromes for near-infrared imaging in mammalsR01GM108579 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2014 to 2017
$1.3M
NCI NIH HHS CA164468NCI NIH HHS P30 CA013330NCI NIH HHS R01 CA164468NIGMS NIH HHS GM073913NIGMS NIH HHS GM108579NIGMS NIH HHS R01 GM073913NIGMS NIH HHS R01 GM105997NIGMS NIH HHS R01 GM108579
6 · The paper itself

Abstract

Fluorescent proteins (FP) are used to study various biological processes. Recently, a series of near-infrared (NIR) FPs based on bacterial phytochromes was developed. Finding ways to improve NIR FPs is becoming progressively important. By applying rational design and molecular evolution we have engineered R. palustris bacterial phytochrome into a single-domain NIR FP of 19.6 kDa, termed GAF-FP, which is 2-fold and 1.4-fold smaller than bacterial phytochrome-based NIR FPs and GFP-like proteins, respectively. Engineering of GAF-FP involved a substitution of 15% of its amino acids and a deletion of the knot structure. GAF-FP covalently binds two tetrapyrrole chromophores, biliverdin (BV) and phycocyanobilin (PCB). With the BV chromophore GAF-FP absorbs at 635 nm and fluoresces at 670 nm. With the PCB chromophore GAF-FP becomes blue-shifted and absorbs at 625 nm and fluoresces at 657 nm. The GAF-FP structure has a high tolerance to small peptide insertions. The small size of GAF-FP and its additional absorbance band in the violet range has allowed for designing a chimeric protein with Renilla luciferase. The chimera exhibits efficient non-radiative energy transfer from luciferase to GAF-FP, resulting in NIR bioluminescence. This study opens the way for engineering of small NIR FPs and NIR luciferases from bacterial phytochromes.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsBiliverdineHeLa CellsHumansLuminescent ProteinsMiceMicroscopy, FluorescenceMolecular Sequence DataMutagenesisPhycobilinsPhycocyaninProtein Structure, TertiaryRhodopseudomonasSequence AlignmentBacterial ProteinsBiliverdineLuminescent ProteinsPhycobilinsPhycocyaninphycocyanobilin

Identifiers

PMID26679720
PMCPMC4683375
OpenAlexW2411339533

What OpenQuestion holds

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LicenceCC BY
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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.