Evidence map›Paper›PMID 25231995›Full record

ArticleThe Journal of biological chemistry2014

Examination of the dimerization states of the single-stranded RNA recognition protein pentatricopeptide repeat 10 (PPR10).

Quanxiu Li, Chuangye Yan, Huisha Xu, Zheng Wang, Jiafu Long, Wenqi Li, Jianping Wu, Ping Yin, Nieng Yan

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Structures of pentatricopeptide repeat proteins.Acta crystallographica. Section F, Structural biology communications · 2026
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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

9 authors.

Quanxiu LiFrom the State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and.
Chuangye YanCenter for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and Ministry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Huisha Xuthe State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China, and.
Zheng Wangthe State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China, and.
Jiafu Longthe State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China, and.
Wenqi LiFrom the State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and.
Jianping WuCenter for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and Ministry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Ping Yinthe National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, and College of Life Sciences and Technology, Huazhong Agricultural University, Wuhan 430070, China yinping@mail.hzau.edu.cn.
Nieng YanFrom the State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and nyan@tsinghua.edu.cn.

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Pentatricopeptide repeat (PPR) proteins, particularly abundant in plastids and mitochrondria of angiosperms, include a large number of sequence-specific RNA binding proteins that are involved in diverse aspects of organelle RNA metabolisms. PPR proteins contain multiple tandom repeats, and each repeat can specifically recognize a RNA base through residues 2, 5, and 35 in a modular fashion. The crystal structure of PPR10 from maize chloroplast exhibits dimeric existence both in the absence and presence of the 18-nucleotide psaJ RNA element. However, previous biochemical analysis suggested a monomeric shift of PPR10 upon RNA binding. In this report, we show that the amino-terminal segments of PPR10 determine the dimerization state of PPR10. A single amino acid alteration of cysteine to serine within repeat 10 of PPR10 further drives dimerization of PPR10. The biochemical elucidation of the determinants for PPR10 dimerization may provide an important foundation to understand the working mechanisms of PPR proteins underlying their diverse physiological functions.

Indexed as

AdenineAmino Acid SequenceArabidopsisChloroplast ProteinsChloroplastsCodonCrystallizationCysteineMolecular Sequence DataNucleic AcidsPlant ProteinsPoint MutationProtein BindingProtein MultimerizationProtein Structure, TertiaryRNA-Binding ProteinsAdenineChloroplast ProteinsCodonCysteineNucleic AcidsPlant ProteinsRNA-Binding ProteinsSerineCell BiologyCrystal StructureProtein-Nucleic Acid InteractionRNARNA Binding ProteinRNA-Protein Interaction

Identifiers

PMID25231995
PMCPMC4223348

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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.