Evidence map›Paper›PMID 38411701›Full record

ArticleMolecular biology reports2024

Increase in the solubility of uvsY using a site saturation mutagenesis library for application in a lyophilized reagent for recombinase polymerase amplification.

Kenta Morimoto, Kevin Maafu Juma, Masaya Yamagata, Teisuke Takita, Kenji Kojima, Koichiro Suzuki, Itaru Yanagihara, Shinsuke Fujiwara, Kiyoshi Yasukawa

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In one paragraph

Article in Molecular biology reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Detection ofJournal of fungi (Basel, Switzerland) · 2026
    Article
  2. Article
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.

Kenta MorimotoDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
Kevin Maafu JumaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
Masaya YamagataDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
Teisuke TakitaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
Kenji KojimaFaculty of Pharmaceutical Sciences, Himeji Dokkyo University, Himeji, Hyogo, 670-8524, Japan.
Koichiro SuzukiThe Research Foundation for Microbial Diseases of Osaka University, Suita, Osaka, 565-0871, Japan.
Itaru YanagiharaDepartment of Developmental Medicine, Research Institute, Osaka Women's and Children's Hospital, Izumi-Shi, Osaka, 594-1101, Japan.
Shinsuke FujiwaraDepartment of Biosciences, School of Biological and Environmental Sciences, Kwansei-Gakuin University, Sanda, Hyogo, 669-1330, Japan.
Kiyoshi YasukawaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan. yasukawa.kiyoshi.7v@kyoto-u.ac.jp.

Funding

Japan Agency for Medical Research and Development 20he0622020h0001Japan Science and Technology Agency JPMJTR20UUJapan Society for the Promotion of Science 22H03332Japan Society for the Promotion of Science 23KJ1201
6 · The paper itself

Abstract

backgroundRecombinase uvsY from bacteriophage T4, along with uvsX, is a key enzyme for recombinase polymerase amplification (RPA), which is used to amplify a target DNA sequence at a constant temperature. uvsY, though essential, poses solubility challenges, complicating the lyophilization of RPA reagents. This study aimed to enhance uvsY solubility.

methodsOur hypothesis centered on the C-terminal region of uvsY influencing solubility. To test this, we generated a site-saturation mutagenesis library for amino acid residues Lys91-Glu134 of the N-terminal (His)

resultsScreening 480 clones identified A116H as the variant with superior solubility. Lyophilized RPA reagents featuring the uvsY variant A116H demonstrated enhanced performance compared to those with wild-type uvsY.

conclusionsThe uvsY variant A116H emerges as an appealing choice for RPA applications, offering improved solubility and heightened lyophilization feasibility.

Indexed as

Amino AcidsRecombinasesGene LibraryMutagenesisSolubilityAmino AcidsRecombinasesIsothermal DNA amplificationRecombinase polymerase amplification (RPA)Site saturation mutagenesis libraryuvsY

Identifiers

PMID38411701
PMCPMC10899321

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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.