Purification and characterization of a novel acid-soluble nuclear protein from developing embryos of the camel tick Hyalomma dromedarii (Acarina: Ixodidae).
A novel acid-soluble protein has been extracted from nuclei of developing embryos of H. dromedarii ticks and purified to homogeneity. This tick embryo basic protein (TEBP) was predominant during the cleavage stage of tick embryogenesis, whereas the complete set of histones was detectable at the late cleavage stage. The amount of TEBP reaches a maximum value at day 9 after oviposition. Thereafter, the original N-terminal dipeptide (leucine-serine) is eliminated. This coincides with the start of organogenesis. In spite of its low molecular mass, TEBP seems to be related to histone H1 in some properties such as solubility in perchloric acid and binding affinity to DNA. A task for the future will be to define the role of this protein as a counterpart of the histones for the genome organization during embryogenesis.
Ibrahim
M A
MA
Fakultät für Biologie, Universität Konstanz, Germany.
Hamed
R R
RR
Rasched
I
I
D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins; D002162:Camelus / Q000469:parasitology*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000302:isolation & purification*; D013987:Ticks / Q000196:embryology*
D060829:Arthropod Proteins; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; C093898:TEBP protein, Hyalomma dromedarii