Evidence map›Paper›PMID 8413253›Full record

ArticleMolecular and cellular biology1993

Binding of a phosphoprotein to the 3' untranslated region of the mouse protamine 2 mRNA temporally represses its translation.

Y K Kwon, N B Hecht

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

36 citing papers in PubMed, 157 citations in OpenAlex.

  1. Bovine Spermatogenesis.Advances in anatomy, embryology, and cell biology · 2025
    Review
  2. Article
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  11. The sperm nucleus: chromatin, RNA, and the nuclear matrix.Reproduction (Cambridge, England) · 2011
    Review
  12. Dendritic trafficking of BDNF mRNA is mediated by translin and blocked by the G196A (Val66Met) mutation.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  13. Behavioral and neurochemical alterations in mice lacking the RNA-binding protein translin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006
    Article
  14. RNA transport and local control of translation.Annual review of cell and developmental biology · 2005
    Review
  15. Article
  16. Review
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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

2 authors at 1 institution in 1 country.

Y K KwonDepartment of Biology, Tufts University, Medford, Massachusetts 02155.
N B Hecht
Tufts University · US

Funding

GENE EXPRESSION DURING SPERMATOGENESISR01GM029224 · NIGMS · TUFTS UNIVERSITY MEDFORD · PI HECHT, NORMAN B · 1985 to 1990
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NIGMS NIH HHS GM 29224
6 · The paper itself

Abstract

The synthesis of the protamines, the predominant nuclear proteins of mammalian spermatozoa, is regulated during germ cell development by mRNA storage for about 7 days in the cytoplasm of differentiating spermatids. Two highly conserved sequences, the Y and H elements present in the 3' untranslated regions (UTRs) of all known mammalian protamine mRNAs, form RNA-protein complexes and specifically bind a protein of 18 kDa. Here, we show that translation of fusion mRNAs was markedly repressed in reticulocyte lysates supplemented with a mouse testis extract enriched for the 18-kDa protein when the mRNAs contained the 3' UTR of mouse protamine 2 (mP2) or the Y and H elements of mP2. No significant decrease was seen when the fusion mRNAs contained the 3' UTR of human growth hormone. The 18-kDa protein is developmentally regulated in male germ cells, requires phosphorylation for RNA binding, and is found in the ribonucleoprotein particle fractions of a testicular postmitochondrial supernatant. We propose that a phosphorylated 18-kDa protein plays a primary role in repressing translation of mP2 mRNA by interaction with the highly conserved Y and H elements. At a later stage of male gamete differentiation, the 18-kDa protein no longer binds to the mRNA, likely as a result of dephosphorylation, enabling the protamine mRNA to be translated.

Indexed as

Protein BiosynthesisAnimalsBase SequenceCell-Free SystemCytoplasmDNAHumansIntronsMaleMiceMolecular Sequence DataPhosphoproteinsProtaminesProtein BindingRibonucleoproteinsRNA, MessengerDNAPhosphoproteinsprotamine 2ProtaminesRibonucleoproteinsRNA, Messenger

Identifiers

PMID8413253
PMCPMC364714
OpenAlexW1918118064

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.