Evidence map›Paper›PMID 29235492›Full record

ArticleScientific reports2017

Proteome-wide Analysis of Lysine 2-hydroxyisobutyrylation in Developing Rice (Oryza sativa) Seeds.

Xiaoxi Meng, Shihai Xing, Loida M Perez, Xiaojun Peng, Qingyong Zhao, Edilberto D Redoña, Cailin Wang, Zhaohua Peng

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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Global Analysis of Lysine Lactylation of Germinated Seeds in Wheat.International journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Global Profiling of 2-hydroxyisobutyrylome in Common Wheat.Genomics, proteomics & bioinformatics · 2022
    Article
  11. Review
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  15. Article
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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

8 authors at 5 institutions in 2 countries.

Xiaoxi MengDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville, Mississippi, 39762, USA.
Shihai XingDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville, Mississippi, 39762, USA.
Loida M PerezDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville, Mississippi, 39762, USA.
Xiaojun PengDepartment of Bioinformatics, Jingjie PTM Biolab Co. Ltd, Hangzhou, 310018, China.
Qingyong ZhaoInstitute of Crop Sciences, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China.
Edilberto D RedoñaDelta Research and Extension Center, Stoneville, P.O. Box 197, Mississippi, 38776, USA.
Cailin WangInstitute of Crop Sciences, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China. clwang@jaas.ac.cn.
Zhaohua PengDepartment of Biochemistry, Molecular Biology, Entomology and Plant Pathology, Mississippi State University, Starkville, Mississippi, 39762, USA. zp7@BCH.msstate.edu.
Mississippi State University · USInstitute of Crop Sciences · CNJiangsu Academy of Agricultural Sciences · CNMississippi Delta Community College · USNew England Biolabs (China) · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine 2-hydroxyisobutyrylation is a recently identified protein post-translational modification that is known to affect the association between histone and DNA. However, non-histone protein lysine 2-hydroxyisobutyrylation remains largely unexplored. Utilizing antibody-based affinity enrichment and nano-HPLC/MS/MS analyses of 2-hydroxyisobutyrylation peptides, we efficaciously identified 9,916 2-hydroxyisobutyryl lysine sites on 2,512 proteins in developing rice seeds, representing the first lysine 2-hydroxyisobutyrylome dataset in plants. Functional annotation analyses indicated that a wide variety of vital biological processes were preferably targeted by lysine 2-hydroxyisobutyrylation, including glycolysis/gluconeogenesis, TCA cycle, starch biosynthesis, lipid metabolism, protein biosynthesis and processing. Our finding showed that 2-hydroxyisobutyrylated histone sites were conserved across plants, human, and mouse. A number of 2-hydroxyisobutyryl sites were shared with other lysine acylations in both histone and non-histone proteins. Comprehensive analysis of the lysine 2-hydroxyisobutyrylation sites illustrated that the modification sites were highly sequence specific with distinct motifs, and they had less surface accessibility than other lysine residues in the protein. Overall, our study provides the first systematic analysis of lysine 2-hydroxyisobutyrylation proteome in plants, and it serves as an important resource for future investigations of the regulatory mechanisms and functions of lysine 2-hydroxyisobutyrylation.

Indexed as

Protein Processing, Post-TranslationalProteomeGene Expression Regulation, DevelopmentalGene Expression Regulation, PlantLysineOryzaPlant ProteinsProteomicsSeeds2-hydroxyisobutyryl-lysineLysinePlant ProteinsProteome

Identifiers

PMID29235492
PMCPMC5727541
OpenAlexW2774442672

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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.