Document Detail


HANP1/H1T2, a novel histone H1-like protein involved in nuclear formation and sperm fertility.
MedLine Citation:
PMID:  16055721     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Hiromitsu Tanaka; Naoko Iguchi; Ayako Isotani; Kouichi Kitamura; Yoshiro Toyama; Yasuhiro Matsuoka; Masayoshi Onishi; Kumiko Masai; Mamiko Maekawa; Kiyotaka Toshimori; Masaru Okabe; Yoshitake Nishimune
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  25     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2005 Aug 
Date Detail:
Created Date:  2005-08-01     Completed Date:  2005-09-09     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7107-19     Citation Subset:  IM    
Affiliation:
Department of Science for Laboratory Animal Experimentation, Research Institute for Microbial Diseases, Osaka University, Suita, Japan.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / chemistry,  metabolism
Amino Acid Sequence
Animals
Arginine / chemistry
Base Sequence
Binding Sites
Cell Differentiation
Cell Nucleus / metabolism*
Chromatin / metabolism
DNA / metabolism
DNA, Complementary / metabolism
DNA-Binding Proteins / chemistry,  genetics*,  physiology*
Dose-Response Relationship, Drug
Epididymis / metabolism
Female
Fertility*
Fertilization
Genetic Vectors
Guanosine Triphosphate / chemistry
Haploidy
Heterozygote
Histones / metabolism*
Homozygote
Male
Mice
Mice, Knockout
Microscopy, Electron
Models, Genetic
Molecular Sequence Data
Mutation
Nuclear Proteins / chemistry,  genetics*,  physiology*
Phylogeny
Protamines / metabolism
Protein Binding
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Spermatids / metabolism
Spermatozoa / metabolism*
Testis / metabolism
Time Factors
Tissue Distribution
Chemical
Reg. No./Substance:
0/Chromatin; 0/DNA, Complementary; 0/DNA-Binding Proteins; 0/H1T2 protein, mouse; 0/Histones; 0/Nuclear Proteins; 0/Prm1 protein, mouse; 0/Protamines; 0/protamine 2; 56-65-5/Adenosine Triphosphate; 74-79-3/Arginine; 86-01-1/Guanosine Triphosphate; 9007-49-2/DNA
Comments/Corrections

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