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A unique vertebrate histone H1-related protamine-like protein results in an unusual sperm chromatin organization
- Source :
- FEBS Journal. 273:4548-4561
- Publication Year :
- 2006
- Publisher :
- Wiley, 2006.
-
Abstract
- Protamine-like proteins constitute a group of sperm nuclear basic proteins that have been shown to be related to somatic linker histones (histone H1 family). Like protamines, they usually replace the chromatin somatic histone complement during spermiogenesis; hence their name. Several of these proteins have been characterized to date in invertebrate organisms, but information about their occurrence and characterization in vertebrates is still lacking. In this sense, the genus Mullus is unique, as it is the only known vertebrate that has its sperm chromatin organized by virtually only protamine-like proteins. We show that the sperm chromatin of this organism is organized by two type I protamine-like proteins (PL-I), and we characterize the major protamine-like component of the fish Mullus surmuletus (striped red mullet). The native chromatin structure resulting from the association of these proteins with DNA was studied by micrococcal nuclease digestion as well as electron microscopy and X-ray diffraction. It is shown that the PL-I proteins organize chromatin in parallel DNA bundles of different thickness in a quite distinct arrangement that is reminiscent of the chromatin organization of those organisms that contain protamines (but not histones) in their sperm.
- Subjects :
- Male
Histone-modifying enzymes
Mytilus edulis
Molecular Sequence Data
Biology
Biochemistry
Histones
Non-histone protein
X-Ray Diffraction
Histone H1
Histone H2A
Animals
Histone code
Nucleosome
Amino Acid Sequence
Protamines
Molecular Biology
Genetics
Nuclear Proteins
DNA
Cell Biology
ChIP-on-chip
Spermatozoa
Chromatin
Perciformes
Cell biology
Subjects
Details
- ISSN :
- 17424658 and 1742464X
- Volume :
- 273
- Database :
- OpenAIRE
- Journal :
- FEBS Journal
- Accession number :
- edsair.doi.dedup.....b75fbb0542294aed4393ea5df17d41ab
- Full Text :
- https://doi.org/10.1111/j.1742-4658.2006.05461.x