Evidence map›Paper›PMID 16055721›Full record

ArticleMolecular and cellular biology2005

HANP1/H1T2, a novel histone H1-like protein involved in nuclear formation and sperm fertility.

Hiromitsu Tanaka, Naoko Iguchi, Ayako Isotani, Kouichi Kitamura, Yoshiro Toyama, Yasuhiro Matsuoka, Masayoshi Onishi, Kumiko Masai, Mamiko Maekawa, Kiyotaka Toshimori and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

52 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. International journal of molecular sciences · 2024
    Article
  6. Review
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  8. Article
  9. Loss-of-function mutations inScience advances · 2022
    Article
  10. Article
  11. Article
  12. Histone variants at a glance.Journal of cell science · 2021
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
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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

12 authors at 3 institutions in 1 country.

Hiromitsu TanakaDepartment of Science for Laboratory Animal Experimentation, Research Institute for Microbial Diseases, Osaka University, Suita, Japan.
Naoko Iguchi
Ayako Isotani
Kouichi Kitamura
Yoshiro Toyama
Yasuhiro Matsuoka
Masayoshi Onishi
Kumiko Masai
Mamiko Maekawa
Kiyotaka Toshimori
Masaru Okabe
Yoshitake Nishimune
Microbial Chemistry Research Foundation · JPChiba University · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We cloned a testis-specific cDNA from mice that encodes a histone H1-like, haploid germ cell-specific nuclear protein designated HANP1/H1T2. The HANP1/H1T2 protein was specifically localized to the nuclei of murine spermatids during differentiation steps 5 to 13 but not to the nuclei of mature sperm. HANP1/H1T2 contains an arginine-serine-rich domain and an ATP/GTP binding site, and it binds to DNA, ATP, and protamine. To investigate the physiological role of HANP1/H1T2, we generated Hanp1/H1T2-disrupted mutant mice. Homozygous Hanp1/H1T2 mutant males were infertile, but females were fertile. Although a substantial number of sperm were recovered from the epididymides, their shape and function were abnormal. During sperm morphogenesis, the formation of nuclei was disturbed and protamine-1 and -2 were only weakly detectable in the nuclei. The chromatin packaging was aberrant, as demonstrated by electron microscopy and biochemical analysis. The mutant sperm exhibited deficient motility and were not competent to fertilize eggs under in vitro fertilization conditions; however, they were capable of fertilizing eggs via intracytoplasmic sperm injection that resulted in the birth of healthy progeny. Thus, we found that HANP1/H1T2 is essential for nuclear formation in functional spermatozoa and is specifically involved in the replacement of histones with protamines during spermiogenesis. At the time of submission of the manuscript, we found an independent publication by Martianov et al. (I. Martianov, S. Brancorsini, R. Catena, A. Gansmuller, N. Kotaja, M. Parvinen, P. Sassone-Corsi, and I. Davidson, Proc. Natl. Acad. Sci. USA 102:2808-2813, 2005) that reported similar results.

Indexed as

FertilityAdenosine TriphosphateAmino Acid SequenceAnimalsArginineBase SequenceBinding SitesCell DifferentiationCell NucleusChromatinDNADNA-Binding ProteinsDNA, ComplementaryDose-Response Relationship, DrugEpididymisFemaleAdenosine TriphosphateArginineChromatinDNADNA-Binding ProteinsDNA, ComplementaryGuanosine TriphosphateH1T2 protein, mouseHistonesNuclear ProteinsPrm1 protein, mouseprotamine 2Protamines

Identifiers

PMID16055721
PMCPMC1190238
OpenAlexW2124412304

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.