Evidence map›Paper›PMID 40817208›Full record

ArticleBMC plant biology2025

Research on the GST gene family in Salix lindleyana reveals Trp162 and Pro202 as key amino acids controlling the release rate of GS-X.

Nan Xu, Yu-Wen Wang, Chang Qu, Zhao-Qun Wu, Xiu-Xing Zhang, Shi-Yi Wang, Ye-Bo Yang, Jing Xue, Hai-Ling Yang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC plant biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Nan Xu *State Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China.
Yu-Wen Wang *State Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China.
Chang Qu *State Key Laboratory of Tree Genetics and Breeding, Chinese Academy of Forestry, Beijing, 100091, China.
Zhao-Qun WuState Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China.
Xiu-Xing ZhangState Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China.
Shi-Yi WangState Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China.
Ye-Bo YangState Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China.
Jing XueState Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China.
Hai-Ling YangState Key Laboratory of Tree Genetics and Breeding, National Engineering Research Center of Tree Breeding and Ecological Restoration, Beijing Forestry University, Beijing, 100083, China. yhailing77@bjfu.edu.cn.

Funding

National Natural Science Foundation of China 32071486STI2030-Major Projects No.2023ZD04057
6 · The paper itself

Abstract

The adaptive evolution of the glutathione S-transferase (GST) gene family in Salix lindleyana provides insights into the relationship between enzyme structure and function. In this study, 37 genes encoding the GST protein were cloned from S. lindleyana with no genomic data available, and their expression levels and enzyme activity were determined in vitro. The 22 genes encoding the Tau GST subfamily were divided into Clades A and B, with Clade A subjected to more relaxed selection pressure than Clade B. Clade A was split into two smaller branches, Clades a and b. Three genes under positive selection from Clade a were chosen for 36 site-directed mutations, with Trp162 and Pro202 crucially affecting variations in GST enzyme activity. Crystal structure analysis of SliGSTU7 complexed with GSH revealed that the Trp162 residue was located at the bottom of the hydrophobic cavity. Homology modeling and molecular docking revealed that the W162G/P202A mutation in SliGSTU7 significantly reduced the neighboring effect during the formation of GS-DNB. A study of the GST gene family of S. lindleyana identified Trp162 and Pro202 as key amino acids that regulate the release rate of GS-X.

Indexed as

Glutathione TransferasePlant ProteinsSalixAmino Acid SequenceMolecular Docking SimulationMultigene FamilyPhylogenyProlineTryptophanGlutathione TransferasePlant ProteinsProlineTryptophanCrystal structureEfficient catalytic mechanismGlutathione transferasePositive selection geneSalix lindleyanaSite-directed mutation

Identifiers

PMID40817208
PMCPMC12357412

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.