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pmid:27833854

Human promyelocytic leukemia protein is targeted to distinct subnuclear domains in plant nuclei and colocalizes with nucleolar constituents in a SUMO-dependent manner.

Christian E Lamm · Myriam Scherer · Nina Reuter · Bushra Amin · Thomas Stamminger · Uwe Sonnewald

FEBS open bio · 2016 doi:10.1002/2211-5463.12134

Paper

complete

Experiment

complete

Data

partial

Analysis

complete

Execution

absent

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Record details sci_version · id · kind · revision · content_hash · schema · created_at · updated_at · generator
id
pmid:27833854
kind
science-record
content_hash
sha256:53de9ed31690fbd524c8f552ec173a45bce0b7c8882eea711941755759f99ea0
schema
https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json
created_at
2026-11-01T15:40:21Z
updated_at
2026-11-01T21:20:43Z
generator object · 2 fields
name
corpus-assay-engine
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paper object · 10 fields
state
complete
title
Human promyelocytic leukemia protein is targeted to distinct subnuclear domains in plant nuclei and colocalizes with nucleolar constituents in a SUMO-dependent manner.
doi
10.1002/2211-5463.12134
pmid
27833854
authors array · 6 items
[0]
Christian E Lamm
[1]
Myriam Scherer
[2]
Nina Reuter
[3]
Bushra Amin
[4]
Thomas Stamminger
[5]
Uwe Sonnewald
journal
FEBS open bio
year
2016
abstract
Eukaryotic nuclei are subdivided into subnuclear structures. Among the most prominent of these structures are the nucleolus and the PML nuclear bodies (PML-NBs). PML-NBs are spherical multiprotein aggregates of varying size localized in the interchromosomal area. PML-NB formation is dependent on the presence of the promyelocytic leukemia protein (PML) as well as on post-translational modification of core components by covalent attachment of the small ubiquitin-like modifier (SUMO). So far, PML-NBs as well as PML have been described in mammalian cells only, whereas no orthologs are known in the plant kingdom. In order to investigate conserved mechanisms in PML targeting, we expressed human PML (hPML) fused to the GFP in Nicotiana benthamiana. Using confocal laser scanning microscopy and coimmunoprecipitation followed by mass spectrometric analysis, we found the fusion protein in association with nucleolar constituents. Importantly, mutants of hPML, which are no longer SUMOylated, showed altered localizations, implying SUMO-dependent targeting of hPML in plants as has previously been shown for mammalian cells. Interestingly, in the presence of proteasome inhibitors, hPML could also be found in the nucleolus of mammalian cells suggesting conserved targeting mechanisms of PML across kingdoms. Finally, Solanum tuberosum COP1, a proposed PML-like protein from plants, was fused to the red fluorescent protein (RFP) and coexpressed with hPML::eGFP. Microscopic analysis confirmed the localization of COP1::RFP in nuclear speckles. However, hPML::eGFP did not colocalize with COP1::RFP. Hence, we conclude that plants do not possess specialized PML-NBs, but that their functions may be covered by other subnuclear structures like the nucleolus. Database Proteomics data have been deposited to the ProteomeXchange Consortium with the identifier PXD004254.
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Statistical analysis of colocalization was carried out using Pearson's correlation coefficient as calculated by the las af software (Leica Microsystems) for Z‐stack micrographs covering the whole nucleus.
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sections[14] "Transient expression in primary human fibroblast, N. benthamiana, and confocal laser scanning microscopy" paragraph 2
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Statistical analysis of colocalization was carried out using Pearson's correlation coefficient as calculated by the las af software (Leica Microsystems) for Z‐stack micrographs covering the whole nucleus.
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All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.
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sections[18] "Nano‐LC‐MS/MS analysis" paragraph 2
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All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.
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Read the published estimate from the source
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All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.
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All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.
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title
Identification of potential human PML interacting proteins in Nicotiana benthamiana
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2026-10-31T18:35:55Z
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Nuclear Nicotiana benthamiana proteins identified as potential PML interactors via immunoprecipitation. Description and Accession number adopted from the N. benthamiana protein database, Best BLAST hit in Arabidopsis shows the respective locus identifier, Associated human PML interactor indicates proteins that interact with PML in mammalian cells as stated in the respective References
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Human PML is targeted to interchromosomal subnuclear domains and interacts with nuclear and nucleolar proteins in planta
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Table 1
caption
Nuclear Nicotiana benthamiana proteins identified as potential PML interactors via immunoprecipitation. Description and Accession number adopted from the N. benthamiana protein database, Best BLAST hit in Arabidopsis shows the respective locus identifier, Associated human PML interactor indicates proteins that interact with PML in mammalian cells as stated in the respective References
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[0] array · 6 items
[0]
Description
[1]
Accession Number N. benthamiana database
[2]
Best BLAST hit Arabidopsis
[3]
Annotated localization
[4]
Associated human PML interactor
[5]
Reference
[1] array · 6 items
[0]
Nuclear pore complex protein NUP85
[1]
Niben101Scf01611g04026.1
[2]
AT4G32910
[3]
Nuclear Pore Complex
[4]
[5]
[2] array · 6 items
[0]
ATP‐dependent RNA helicase
[1]
Niben101Scf06884 g00001.1
[2]
AT5G62190
[3]
Nucleolus
[4]
[5]
[3] array · 6 items
[0]
Holliday junction ATP‐dependent DNA helicase RuvB
[1]
Niben101Scf01281 g02006.1
[2]
AT5G67630
[3]
Nucleolus
[4]
[5]
[4] array · 6 items
[0]
Importin subunit alpha
[1]
Niben101Scf03390 g08002.1
[2]
AT3G06720
[3]
Nucleolus
[4]
[5]
[5] array · 6 items
[0]
Nucleolar protein 16
[1]
Niben101Scf04623 g02007.1
[2]
AT1G02870
[3]
Nucleolus
[4]
[5]
[6] array · 6 items
[0]
Replication factor C subunit 3
[1]
Niben101Scf01888 g07004.1
[2]
AT1G21690
[3]
Nucleolus
[4]
Replication factor C4
[5]
McNamara et al. 33
[7] array · 6 items
[0]
Replication factor C subunit 3
[1]
Niben101Scf02197 g01014.1
[2]
AT1G77470
[3]
Nucleolus
[4]
Replication factor C4
[5]
McNamara et al. 33
[8] array · 6 items
[0]
Ribosomal RNA large subunit methyltransferase
[1]
Niben101Scf23821 g00012.1
[2]
AT3G28460
[3]
Nucleolus
[4]
[5]
[9] array · 6 items
[0]
RNA‐binding protein like
[1]
Niben101Scf15360 g00006.1
[2]
AT4G32720
[3]
Nucleolus
[4]
[5]
[10] array · 6 items
[0]
2‐oxoglutarate (2OG) and Fe(II)‐dependent oxygenase superfamily protein
[1]
Niben101Scf06267 g03010.1
[2]
AT2G17970
[3]
Nucleus
[4]
[5]
[11] array · 6 items
[0]
65‐kDa microtubule‐associated protein 6
[1]
Niben101Scf07839 g00002.1
[2]
AT2G01910
[3]
Nucleus
[4]
Microtubule‐associated protein 1 light chain 3 beta
[5]
He et al. 40
[12] array · 6 items
[0]
ATP‐dependent RNA helicase
[1]
Niben101Scf05387 g09003.1
[2]
AT3G06980
[3]
Nucleus
[4]
[5]
[13] array · 6 items
[0]
DNA‐directed RNA polymerase subunit D
[1]
Niben101Scf00414 g09001.1
[2]
AT1G60620
[3]
Nucleus
[4]
DNA‐directed RNA polymerase POLR2E
[5]
Ravasi et al. 35
[14] array · 6 items
[0]
FRIGIDA‐like protein 3
[1]
Niben101Scf04181 g00024.1
[2]
AT5G48385
[3]
Nucleus
[4]
[5]
[15] array · 6 items
[0]
Heavy metal transport/detoxification superfamily protein
[1]
Niben101Scf07109 g05004.1
[2]
AT4G35060
[3]
Nucleus
[4]
[5]
[16] array · 6 items
[0]
Histone‐lysine N‐methyltransferase
[1]
Niben101Scf01020 g00014.1
[2]
AT5G04940
[3]
Nucleus
[4]
Histone‐lysine N‐methyltransferase G9a
[5]
Lusic et al. 34
[17] array · 6 items
[0]
Histone‐lysine N‐methyltransferase 2A
[1]
Niben101Scf12382 g00017.1
[2]
AT1G73100
[3]
Nucleus
[4]
Histone‐lysine N‐methyltransferase G9a
[5]
Lusic et al., 34
[18] array · 6 items
[0]
Holliday junction ATP‐dependent DNA helicase RuvB
[1]
Niben101Scf04267 g00016.1
[2]
AT5G27740
[3]
Nucleus
[4]
Replication factor C4
[5]
McNamara et al. 33
[19] array · 6 items
[0]
Nuclear cap‐binding protein subunit 1
[1]
Niben101Scf07629 g00001.1
[2]
AT2G13540
[3]
Nucleus
[4]
[5]
[20] array · 6 items
[0]
Plastid transcriptionally active 12
[1]
Niben101Scf08698 g02020.1
[2]
AT2G34640
[3]
Nucleus
[4]
[5]
[21] array · 6 items
[0]
Protein IQ‐DOMAIN 31
[1]
Niben101Scf06172 g01003.1
[2]
AT1G74690
[3]
Nucleus
[4]
[5]
[22] array · 6 items
[0]
Protein IQ‐DOMAIN 31
[1]
Niben101Scf01326 g08021.1
[2]
AT1G74690
[3]
Nucleus
[4]
[5]
[23] array · 6 items
[0]
Replication factor C subunit 3
[1]
Niben101Scf07391 g04027.1
[2]
AT1G63160
[3]
Nucleus
[4]
Replication factor C4
[5]
McNamara et al. 33
[24] array · 6 items
[0]
Replication factor C subunit 4
[1]
Niben101Scf01382 g04008.1
[2]
AT5G22010
[3]
Nucleus
[4]
Replication factor C4
[5]
McNamara et al. 33
[25] array · 6 items
[0]
Replication factor C subunit 5
[1]
Niben101Scf05056 g02015.1
[2]
AT1G63160
[3]
Nucleus
[4]
Replication factor C4
[5]
McNamara et al. 33
[26] array · 6 items
[0]
RNA‐binding KH domain‐containing protein
[1]
Niben101Scf03015 g05008.1
[2]
AT5G15270
[3]
Nucleus
[4]
[5]
[27] array · 6 items
[0]
RNA‐binding protein 1
[1]
Niben101Scf06105 g03006.1
[2]
AT4G10110
[3]
Nucleus
[4]
[5]
[28] array · 6 items
[0]
snRK1‐interacting protein 1
[1]
Niben101Scf03949 g06008.1
[2]
AT1G71310
[3]
Nucleus
[4]
RAD51
[5]
Boichuk et al. 38
[29] array · 6 items
[0]
WD‐40 repeat family protein/small nuclear ribonucleoprotein
[1]
Niben101Scf11084 g02025.1
[2]
AT2G41500
[3]
Nucleus
[4]
[5]
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section[6]/table-wrap[1]#feb412134-tbl-0001
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Statistical analysis of colocalization was carried out using Pearson's correlation coefficient as calculated by the las af software (Leica Microsystems) for Z‐stack micrographs covering the whole nucleus.
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All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.
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oscopy and coimmunoprecipitation followed by mass spectrometric analysis, we found the fusion protein in ass
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assay:2
Complete file
{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:27833854", "kind": "science-record", "revision": 6, "content_hash": "sha256:53de9ed31690fbd524c8f552ec173a45bce0b7c8882eea711941755759f99ea0", "created_at": "2026-11-01T15:40:21Z", "updated_at": "2026-11-01T21:20:43Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "Human promyelocytic leukemia protein is targeted to distinct subnuclear domains in plant nuclei and colocalizes with nucleolar constituents in a SUMO-dependent manner.", "doi": "10.1002/2211-5463.12134", "pmid": "27833854", "authors": ["Christian E Lamm", "Myriam Scherer", "Nina Reuter", "Bushra Amin", "Thomas Stamminger", "Uwe Sonnewald"], "journal": "FEBS open bio", "year": 2016, "abstract": "Eukaryotic nuclei are subdivided into subnuclear structures. Among the most prominent of these structures are the nucleolus and the PML nuclear bodies (PML-NBs). PML-NBs are spherical multiprotein aggregates of varying size localized in the interchromosomal area. PML-NB formation is dependent on the presence of the promyelocytic leukemia protein (PML) as well as on post-translational modification of core components by covalent attachment of the small ubiquitin-like modifier (SUMO). So far, PML-NBs as well as PML have been described in mammalian cells only, whereas no orthologs are known in the plant kingdom. In order to investigate conserved mechanisms in PML targeting, we expressed human PML (hPML) fused to the GFP in Nicotiana benthamiana. Using confocal laser scanning microscopy and coimmunoprecipitation followed by mass spectrometric analysis, we found the fusion protein in association with nucleolar constituents. Importantly, mutants of hPML, which are no longer SUMOylated, showed altered localizations, implying SUMO-dependent targeting of hPML in plants as has previously been shown for mammalian cells. Interestingly, in the presence of proteasome inhibitors, hPML could also be found in the nucleolus of mammalian cells suggesting conserved targeting mechanisms of PML across kingdoms. Finally, Solanum tuberosum COP1, a proposed PML-like protein from plants, was fused to the red fluorescent protein (RFP) and coexpressed with hPML::eGFP. Microscopic analysis confirmed the localization of COP1::RFP in nuclear speckles. However, hPML::eGFP did not colocalize with COP1::RFP. Hence, we conclude that plants do not possess specialized PML-NBs, but that their functions may be covered by other subnuclear structures like the nucleolus. Database Proteomics data have been deposited to the ProteomeXchange Consortium with the identifier PXD004254.", "claims": [{"id": "claim-method", "statement": "Statistical analysis of colocalization was carried out using Pearson's correlation coefficient as calculated by the las af software (Leica Microsystems) for Z‐stack micrographs covering the whole nucleus.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:27833854", "locator": "sections[14] \"Transient expression in primary human fibroblast, N. benthamiana, and confocal laser scanning microscopy\" paragraph 2", "quote": "Statistical analysis of colocalization was carried out using Pearson's correlation coefficient as calculated by the las af software (Leica Microsystems) for Z‐stack micrographs covering the whole nucleus."}], "state": "complete"}, {"id": "claim-data-access", "statement": "All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:27833854", "locator": "sections[18] \"Nano‐LC‐MS/MS analysis\" paragraph 2", "quote": "All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "complete", "objective": null, "steps": [{"id": "read_published_estimate", "order": 1, "name": "Read the published estimate from the source", "kind": "other", "state": "complete", "blocked_on": null, "description": "The claim, method and evidence span published with the source article.", "duration_hours": null, "parameters": {}, "inputs": ["source:pmid:27833854"], "outputs": ["the published estimate and its evidence"], "instruments": [], "reagents": []}, {"id": "obtain_source_data", "order": 2, "name": "Obtain the source data from the named repository", "kind": "data-preparation", "state": "complete", "blocked_on": null, "description": "The GEO series accession resolves and its sample accessions are listed. This lane did not download the dataset or read its licence.", "duration_hours": null, "parameters": {}, "inputs": ["data:geo:PXD004254"], "outputs": ["the source data with its repository provenance"], "instruments": [], "reagents": []}, {"id": "run_analysis", "order": 3, "name": "Run the published analysis", "kind": "analysis", "state": "complete", "blocked_on": null, "description": "Apply the paper's statistical method to the resolved series and compare the result with the published target.", "duration_hours": null, "parameters": {}, "inputs": ["data:geo:PXD004254"], "outputs": ["the replicated result and its comparison"], "instruments": [], "reagents": []}], "materials": [], "instruments": [], "reagents": [], "conditions": {}, "gaps": []}, "data": {"state": "partial", "assets": [{"id": "source:pmid:27833854", "role": "manuscript", "format": "xml", "media_type": "application/xml", "uri": "https://doi.org/10.1002/2211-5463.12134", "sha256": "sha256:cd914c48883e38f302c9eaf3bac3d24da478603b1c1d55974c6845c4357db165", "bytes": 50542, "access": "open", "state": "resolved", "reader": null, "reader_status": "reader_required", "identifier": "10.1002/2211-5463.12134", "version": null, "note": "Full article fetched from PMC; the checksum covers the rendered section body, not the original XML bytes.", "structure": {"pmcid": "PMC5095151", "source": "europe_pmc_fulltext", "coverage": "whole_body", "text_hash_scope": "rendered_section_body"}}, {"id": "data:geo:PXD004254", "role": "raw", "format": "geo-series", "media_type": "application/vnd.ncbi.geo-series+json", "uri": "https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=PXD004254", "sha256": null, "bytes": null, "access": "open", "state": "resolved", "reader": null, "reader_status": "reader_required", "identifier": "PXD004254", "version": null, "note": "All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.", "structure": {"repository": "GEO", "access_route": "GEO accession URL", "access_statement_verbatim": "All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254.", "access_statement_kind": "data_availability_statement", "sample_accessions": [], "sample_count": null, "group_sizes": null, "group_sizes_basis": null, "platform": null, "taxon": null, "title": "Identification of potential human PML interacting proteins in Nicotiana benthamiana", "resolution_checked_at": "2026-10-31T18:35:55Z", "resolution_check": "identifier_resolution_only_no_download_no_licence_read", "downloaded": false, "licence_read": false}}, {"id": "asset:table:pmid:27833854:1", "role": "table", "format": "jats-table", "media_type": "application/vnd.jats.table+json", "uri": null, "sha256": "sha256:3d02b3532b182107d9ca9596f33147212652f183d4b1545298233a752716dafe", "bytes": 4041, "access": "open", "state": "verified", "reader": "read_table", "reader_status": "available", "identifier": "section[6]/table-wrap[1]#feb412134-tbl-0001", "version": null, "note": "Nuclear Nicotiana benthamiana proteins identified as potential PML interactors via immunoprecipitation. Description and Accession number adopted from the N. benthamiana protein database, Best BLAST hit in Arabidopsis shows the respective locus identifier, Associated human PML interactor indicates proteins that interact with PML in mammalian cells as stated in the respective References", "structure": {"pmcid": "PMC5095151", "section_index": 6, "section_title": "Human PML is targeted to interchromosomal subnuclear domains and interacts with nuclear and nucleolar proteins in planta", "row_count": 30, "column_count": 6}, "table": {"label": "Table 1", "caption": "Nuclear Nicotiana benthamiana proteins identified as potential PML interactors via immunoprecipitation. Description and Accession number adopted from the N. benthamiana protein database, Best BLAST hit in Arabidopsis shows the respective locus identifier, Associated human PML interactor indicates proteins that interact with PML in mammalian cells as stated in the respective References", "rows": [["Description", "Accession Number N. benthamiana database", "Best BLAST hit Arabidopsis", "Annotated localization", "Associated human PML interactor", "Reference"], ["Nuclear pore complex protein NUP85", "Niben101Scf01611g04026.1", "AT4G32910", "Nuclear Pore Complex", "", ""], ["ATP‐dependent RNA helicase", "Niben101Scf06884 g00001.1", "AT5G62190", "Nucleolus", "", ""], ["Holliday junction ATP‐dependent DNA helicase RuvB", "Niben101Scf01281 g02006.1", "AT5G67630", "Nucleolus", "", ""], ["Importin subunit alpha", "Niben101Scf03390 g08002.1", "AT3G06720", "Nucleolus", "", ""], ["Nucleolar protein 16", "Niben101Scf04623 g02007.1", "AT1G02870", "Nucleolus", "", ""], ["Replication factor C subunit 3", "Niben101Scf01888 g07004.1", "AT1G21690", "Nucleolus", "Replication factor C4", "McNamara et al. 33"], ["Replication factor C subunit 3", "Niben101Scf02197 g01014.1", "AT1G77470", "Nucleolus", "Replication factor C4", "McNamara et al. 33"], ["Ribosomal RNA large subunit methyltransferase", "Niben101Scf23821 g00012.1", "AT3G28460", "Nucleolus", "", ""], ["RNA‐binding protein like", "Niben101Scf15360 g00006.1", "AT4G32720", "Nucleolus", "", ""], ["2‐oxoglutarate (2OG) and Fe(II)‐dependent oxygenase superfamily protein", "Niben101Scf06267 g03010.1", "AT2G17970", "Nucleus", "", ""], ["65‐kDa microtubule‐associated protein 6", "Niben101Scf07839 g00002.1", "AT2G01910", "Nucleus", "Microtubule‐associated protein 1 light chain 3 beta", "He et al. 40"], ["ATP‐dependent RNA helicase", "Niben101Scf05387 g09003.1", "AT3G06980", "Nucleus", "", ""], ["DNA‐directed RNA polymerase subunit D", "Niben101Scf00414 g09001.1", "AT1G60620", "Nucleus", "DNA‐directed RNA polymerase POLR2E", "Ravasi et al. 35"], ["FRIGIDA‐like protein 3", "Niben101Scf04181 g00024.1", "AT5G48385", "Nucleus", "", ""], ["Heavy metal transport/detoxification superfamily protein", "Niben101Scf07109 g05004.1", "AT4G35060", "Nucleus", "", ""], ["Histone‐lysine N‐methyltransferase", "Niben101Scf01020 g00014.1", "AT5G04940", "Nucleus", "Histone‐lysine N‐methyltransferase G9a", "Lusic et al. 34"], ["Histone‐lysine N‐methyltransferase 2A", "Niben101Scf12382 g00017.1", "AT1G73100", "Nucleus", "Histone‐lysine N‐methyltransferase G9a", "Lusic et al., 34"], ["Holliday junction ATP‐dependent DNA helicase RuvB", "Niben101Scf04267 g00016.1", "AT5G27740", "Nucleus", "Replication factor C4", "McNamara et al. 33"], ["Nuclear cap‐binding protein subunit 1", "Niben101Scf07629 g00001.1", "AT2G13540", "Nucleus", "", ""], ["Plastid transcriptionally active 12", "Niben101Scf08698 g02020.1", "AT2G34640", "Nucleus", "", ""], ["Protein IQ‐DOMAIN 31", "Niben101Scf06172 g01003.1", "AT1G74690", "Nucleus", "", ""], ["Protein IQ‐DOMAIN 31", "Niben101Scf01326 g08021.1", "AT1G74690", "Nucleus", "", ""], ["Replication factor C subunit 3", "Niben101Scf07391 g04027.1", "AT1G63160", "Nucleus", "Replication factor C4", "McNamara et al. 33"], ["Replication factor C subunit 4", "Niben101Scf01382 g04008.1", "AT5G22010", "Nucleus", "Replication factor C4", "McNamara et al. 33"], ["Replication factor C subunit 5", "Niben101Scf05056 g02015.1", "AT1G63160", "Nucleus", "Replication factor C4", "McNamara et al. 33"], ["RNA‐binding KH domain‐containing protein", "Niben101Scf03015 g05008.1", "AT5G15270", "Nucleus", "", ""], ["RNA‐binding protein 1", "Niben101Scf06105 g03006.1", "AT4G10110", "Nucleus", "", ""], ["snRK1‐interacting protein 1", "Niben101Scf03949 g06008.1", "AT1G71310", "Nucleus", "RAD51", "Boichuk et al. 38"], ["WD‐40 repeat family protein/small nuclear ribonucleoprotein", "Niben101Scf11084 g02025.1", "AT2G41500", "Nucleus", "", ""]], "row_count": 30, "column_count": 6, "numeric_cells": 89, "header_rows": 1, "locator": 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The physical bench the paper used is not, so a physical validation cannot be run here."}, "data": {"tier": "R1", "reachable": true, "accessions": ["PXD004254"], "resolved_accessions": ["PXD004254"], "statements": ["All mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository 65 with the dataset identifier PXD004254."], "basis": "The paper names PXD004254 in ProteomeXchange Consortium via the PRIDE partner repository and the accession resolves in the repository. 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