Evidence map›Paper›PMID 28761138›Full record

ArticleScientific reports2017

An atypical strictosidine synthase, OsSTRL2, plays key roles in anther development and pollen wall formation in rice.

Ting Zou, Shuangcheng Li, Mingxing Liu, Tao Wang, Qiao Xiao, Dan Chen, Qiao Li, Yanling Liang, Jun Zhu, Yueyang Liang and 5 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 48 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

15 authors at 2 institutions in 1 country.

Ting ZouState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Shuangcheng LiState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China. lisc926105@163.com.
Mingxing LiuState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Tao WangState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Qiao XiaoState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Dan ChenState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Qiao LiState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Yanling LiangState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Jun ZhuState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Yueyang LiangState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Qiming DengState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Shiquan WangState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Aiping ZhengState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Lingxia WangState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China.
Ping LiState Key Laboratory of Hybrid Rice, Sichuan Agricultural University, Chengdu, 611130, China. liping6575@163.com.
Rice Research Institute · CNSichuan Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Strictosidine synthase (STR) plays an important role in the biosynthesis of terpenoid indole alkaloids (TIAs) and is expressed in a range of active meristematic tissues of higher plants. STR proteins are involved in different physiological and biochemical pathways. However, the function of STR proteins in rice development remains poorly understood. In this study, we identified 21 possible STR-like (OsSTRL) family members in rice genome and found that only one gene, OsSTRL2, exhibited a pre-emergency specific florescence expression pattern. Tissue-specific expression profile analysis, β-glucuronidase histochemical (GUS) staining and RNA in situ hybridization confirmed that OsSTRL2 was highly expressed in tapetal cells and microspores. Comparative protein sequence analysis indicated that OsSTRL2 lacked the key catalytic residue found in a typical STR (STR1), although it possessed conserved β-propellers and α-helices formed the basic structure of STR1. OsSTRL2 knockout mutant resulted to male sterility because of the defects in anther development and pollen wall formation. Subcellular localization of OsSTRL2-YFP revealed that the OsSTRL2 protein was primarily localized in the endoplasmic reticulum (ER). Therefore, OsSTRL2 is an atypical strictosidine synthase that plays crucial roles in regulating anther development and pollen wall formation in rice.

Indexed as

Carbon-Nitrogen LyasesCatalytic DomainCell WallMutationOryzaPollenPollinationCarbon-Nitrogen Lyasesstrictosidine synthetase

Identifiers

PMID28761138
PMCPMC5537339
OpenAlexW2736710565

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.