Evidence map›Paper›PMID 25992309›Full record

ArticleSpringerPlus2015

Functional and expression analyses of two kinds of betaine aldehyde dehydrogenases in a glycinebetaine-hyperaccumulating graminaceous halophyte, Leymus chinensis.

Shiro Mitsuya, Asumi Tsuchiya, Keiko Kono-Ozaki, Takashi Fujiwara, Teruhiro Takabe, Tetsuko Takabe

Open access · diamondAbstract read
In one paragraph

Article in SpringerPlus, 2015. 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, top 96% 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

2 citing papers in PubMed, 9 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 2 institutions in 1 country.

Shiro MitsuyaGraduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601 Japan.
Asumi TsuchiyaGraduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601 Japan.
Keiko Kono-OzakiGraduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601 Japan.
Takashi FujiwaraGraduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601 Japan.
Teruhiro TakabeResearch Institute, Meijo University, Tenpaku, Nagoya, 464-8502 Japan.
Tetsuko TakabeResearch Institute, Meijo University, Tenpaku, Nagoya, 464-8502 Japan.
Nagoya University · JPMeijo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycinebetaine (GB) is an important compatible solute for salinity tolerance in many plants. In this study, we analyzed the enzymatic activity and the expression level of betaine aldehyde dehydrogenase (BADH), an important enzyme that catalyzes the last step in the GB synthesis in Leymus chinensis, a GB-hyperaccumulating graminaceous halophyte, and compared with those of barley, a graminaceous glycophyte. We have isolated cDNAs for two BADH genes, LcBADH1 and LcBADH2. LcBADH1 has a putative peroxisomal signal peptide (PTS1) at its C-terminus, while LcBADH2 does not have any typical signal peptide. Using immunofluorescent labeling, we showed that BADH proteins were localized to the cytosol and dot-shaped organelles in the mesophyll and bundle sheath cells of L.chinensis leaves. The affinity of recombinant LcBADH2 for betaine aldehyde was comparable to other plant BADHs, whereas recombinant LcBADH1 showed extremely low affinity for betaine aldehyde, indicating that LcBADH2 plays a major role in GB synthesis in L. chinensis. In addition, the recombinant LcBADH2 protein was tolerant to NaCl whereas LcBADH1 wasn't. The kinetics, subcellular and tissue localization of BADH proteins were comparable between L. chinensis and barley. The activity and expression level of BADH proteins were higher in L. chinensis compared with barley under both normal and salinized conditions, which may be related to the significant difference in the amount of GB accumulation between two plants.

Indexed as

BarleyBetaine aldehyde dehydrogenaseCholine monooxygenaseEnzyme kineticsSalinity stressSubcellular localization

Identifiers

PMID25992309
PMCPMC4431990
OpenAlexW2102964991

What OpenQuestion holds

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LicenceCC BY
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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.