Evidence map›Paper›PMID 26161976›Full record

ArticlePloS one2015

Dual Roles of the Lysine-Rich Matrix Protein (KRMP)-3 in Shell Formation of Pearl Oyster, Pinctada fucata.

Jian Liang, Guangrui Xu, Jun Xie, Ilsun Lee, Liang Xiang, Hongzhong Wang, Guiyou Zhang, Liping Xie, Rongqing Zhang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Polyamines Promote Aragonite Nucleation and Generate Biomimetic Structures.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
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  5. The 'Shellome' of the Crocus ClamFrontiers in genetics · 2021
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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 at 1 institution in 1 country.

Jian LiangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Guangrui XuInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Jun XieInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Ilsun LeeInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Liang XiangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Hongzhong WangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Guiyou ZhangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Liping XieInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China; Protein Science Laboratory of the Ministry of Education, Tsinghua University, Beijing, China.
Rongqing ZhangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, China; Protein Science Laboratory of the Ministry of Education, Tsinghua University, Beijing, China.
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix proteins play important roles in shell formation. Our group firstly isolated three cDNAs encoding lysine-rich matrix protein from Pinctada fucata in 2006. However, the functions of KRMPs are not fully understood. In addition, KRMPs contain two functional domains, the basic domain and the Gly/Tyr domain respectively. Based on the modular organization, the roles of their two domains were poorly characterized. Furthermore, KRMPs were then reported in other two species, P. maxima and P. margaritifera, which indicated that KRMPs might be very important for shell formation. In this study, the characterization and function of KRMP-3 and its two functional domains were studied in vitro through purification of recombinant glutathione S-transferase tagged KRMP-3 and two KRMP-3 deletion mutants. Western blot and immunofluorescence revealed that native KRMP-3 existed in the EDTA-insoluble matrix of the prismatic layer and was located in the organic sheet and the prismatic sheath. Recombinant KRMP-3 (rKRMP-3) bound tightly to chitin and this binding capacity was duo to the Gly/Tyr-rich region. rKRMP-3 inhibited the precipitation of CaCO3, affected the crystal morphology of calcite and inhibited the growth of aragonite in vitro, which was almost entirely attributed to the lysine-rich region. The results present direct evidence of the roles of KRMP-3 in shell biomineralization. The functional rBR region was found to participate in the growth control of crystals and the rGYR region was responsible to bind to chitin.

Indexed as

Amino Acid SequenceAnimalsAnimal ShellsCalcium CarbonateChemical PrecipitationChitinConserved SequenceCrystallizationExtracellular Matrix ProteinsMolecular Sequence DataPinctadaProtein BindingProtein TransportSequence Homology, Amino AcidCalcium CarbonateChitinExtracellular Matrix Proteins

Identifiers

PMID26161976
PMCPMC4498902
OpenAlexW1567199036

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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.