Characterization of the histones of Trypanosoma brucei brucei bloodstream forms.
Five groups of histones were shown in Trypanosoma brucei brucei, displaying qualitative and quantitative differences between two stages of the parasite's life-cycle. The influence of the histones of T. b. brucei bloodstream forms on the compaction pattern of the chromatin was investigated and their extractability in diluted acids and their amino acid composition were analysed. While nonhistone proteins barely influenced the formation of higher-order chromatin structures, the histone H1-like proteins were essential for the regular spacing of the nucleosomes and the salt-dependent condensation of the nucleosome filament. Differences were seen in the amino-acid composition of histones of bloodstream forms as compared to procyclic culture forms and higher eukaryotes which may explain the disparities seen in the condensation of the chromatin between the two stages of the life cycle as well as the lack of a salt-dependent condensation into a 30 nm fiber. They point to an alternative method of organizing and processing the genetic information in the nucleus of the trypanosome as compared to higher eukaryotes, the possible hosts of the parasite.
Burri
M
M
Swiss Tropical Institute, Basel.
Schlimme
W
W
Betschart
B
B
Hecker
H
H
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005591:Chemical Fractionation; D002843:Chromatin / Q000737:chemistry; D006657:Histones / Q000737:chemistry*; D009707:Nucleosomes / Q000737:chemistry / Q000648:ultrastructure; D015800:Protozoan Proteins / Q000737:chemistry*; D051381:Rats; D014346:Trypanosoma brucei brucei / Q000737:chemistry* / Q000254:growth & development
D000596:Amino Acids; D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D015800:Protozoan Proteins