Coexistence of two chromatin structures in sperm nuclei of the bivalve mollusc Protothaca thaca.
The chromatin of the spermatozoa from the bivalve mollusc Protothaca thaca, has a peculiar composition in which coexist core histones with sperm-specific proteins H1 and Pt1, the latter being a protein exhibiting features intermediate between histones and protamines. In this paper, we report an analysis of chromatin organization using micrococcal nuclease digestion, salt fractionation of soluble chromatin derived from nuclease digestion and crosslinking experiments. The results obtained indicate that it is possible to obtain two types of chromatin, one which is soluble, more accessible to micrococcal nuclease action and which does not contain Pt1, and another insoluble type, more resistant to micrococcal nuclease and enriched in protein Pt1. The crosslinking experiments show that the protein Pt1 interacts with itself and with core histones but not with sperm-specific H1. These results have led us to propose a special structural arrangement for this chromatin. Based in the data reported here we propose the coexistence in the genome of P. thaca of two interspersed chromatin domains, one nucleosomal and the other nonnucleosomal containing protein Pt1.
Olivares
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C
Departamento Biomedico, Universidad de Antofagasta, Chile.
Lila Vera
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Ruíz-Lara
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S
D000818:Animals; D002467:Cell Nucleus / Q000737:chemistry*; D005591:Chemical Fractionation; D002843:Chromatin / Q000737:chemistry*; D003432:Cross-Linking Reagents; D008297:Male; D008974:Mollusca / Q000737:chemistry*; D009687:Nuclear Proteins / Q000032:analysis*; D012965:Sodium Chloride; D013094:Spermatozoa / Q000737:chemistry* / Q000648:ultrastructure
D002843:Chromatin; D003432:Cross-Linking Reagents; D009687:Nuclear Proteins; D012965:Sodium Chloride