Evidence map›Paper›PMID 11437252›Full record

ArticlePlant molecular biology2001

Identification of a cytoskeleton-associated 120 kDa RNA-binding protein in developing rice seeds.

R Sami-Subbu, S B Choi, Y Wu, C Wang, T W Okita

Abstract read
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In one paragraph

Article in Plant molecular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. mRNA Localization to the Endoplasmic Reticulum in Plant Endosperm Cells.International journal of molecular sciences · 2022
    Review
  4. Article
  5. mRNA Localization in Plant Cells.Plant physiology · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. The Tudor Staphylococcal Nuclease Protein ofFrontiers in cellular and infection microbiology · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Microtubule-associated proteins in higher plants.Journal of plant research · 2007
    Review
  19. Article
  20. Review
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

5 authors at 2 institutions in 2 countries.

R Sami-SubbuInstitute of Biological Chemistry, Washington State University, Pullman 99164-6340, USA.
S B Choi
Y Wu
C Wang
T W Okita
Washington State University · USNational Chemical Laboratory · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During rice seed development, prolamine RNAs are localized to the surface of the prolamine storage protein bodies (PBs), organelles bounded by the endoplasmic reticulum (ER). The exact mechanism by which prolamine RNAs are enriched on this ER subdomain is not known but recent evidence indicates the directed transport and targeting of prolamine RNAs to the prolamine PBs. As such a process involves RNA signal determinants and cytoskeleton-interacting proteins that recognize these signals, we obtained an enriched cytoskeleton-PB fraction and identified a prominent RNA-binding activity, Rp120, by RNA-binding UV-cross-linking assay. Recombinant cDNA clones of Rp120 revealed that the primary sequence shared considerable structural homology to the human transcriptional coactivator p100 and possessed a modular organization, four nucleic acid-binding SN domains, a tudor domain and a coil-coil domain. Consistent with the presence of SN domains, Rp120 binds a variety of RNAs including prolamine RNA. Interaction with the latter RNA, however, was specific as binding activity was evident only to the prolamine 3' UTR and not to the 5' UTR or coding sequences. Rp120 is also able to interact with other proteins as its sedimentation behavior in sucrose density gradient suggests an association with the cytoskeleton. The presence of a tudor domain, suggested to have a role in RNA processing or transport, together with the SN and coiled-coil domains are consistent with the view that Rp120 may be involved in RNA sorting in rice endosperm.

Indexed as

Amino Acid SequenceBinding SitesCytoskeletonImmunoblottingMolecular Sequence DataMolecular WeightOryzaProtein BindingRNA-Binding ProteinsRNA, MessengerSeedsSequence AlignmentSequence Homology, Amino AcidSubcellular FractionsTissue DistributionRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID11437252
OpenAlexW37239255

What OpenQuestion holds

Textmetadata
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.