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Structure of sea urchin sperm chromatin core particle
Journal article   Open access   Peer reviewed

Structure of sea urchin sperm chromatin core particle

R T Simpson and L W Bergman
The Journal of biological chemistry, v 255(22), pp 10702-10709
25 Nov 1980
PMID: 7430146
url
https://doi.org/10.1016/S0021-9258(19)70364-0View
Published, Version of Record (VoR) Open

Abstract

Amino Acids - analysis Animals Base Composition Chickens Chromatin - analysis DNA - analysis Erythrocytes - analysis Histones - analysis Male Molecular Weight Nucleic Acid Conformation Nucleic Acid Denaturation Osmolar Concentration Protein Conformation Sea Urchins Species Specificity Spermatozoa - analysis
Sea urchin sperm chromatin contains forms of H1, H2A, and H2B which differ from those present in adult tissues. We have delineated some effects of the variant H2A and H2B on chromatin by study of the structure of the core particle from Strongylocentrotus purpuratus sperm. The particle contains 145 base pairs of DNA and equal amounts of the four smaller histones. It sediments at 11 S and has a circular dichroism spectrum similar to that of particles containing more typical histones. The sperm core particle undergoes a shape change at low ionic strength, as observed for chicken erythrocyte particles. In contrast to these similarities, the melting profile of the sperm particle is quite different from that of erythrocyte; both the reversible transition and the irreversible denaturation of the core particle occur at higher temperatures. The sperm core particle is digested by DNase I more slowly than the core particle from chicken erythrocyte. Cutting site maps for the sperm core particle reveal the same basic organization of DNA by these histones; however, certain features of the map differ significantly from that for chicken erythrocyte, demonstrating a modulation of the canonical core particle structure by the unusual histones present in sea urchin sperm.

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Biochemistry & Molecular Biology
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