Phosphate content of goose erythrocyte histones

Abstract

Although chromatographic profiles and amino acid compositions of erythrocyte histones from normal and regenerating goose blood did not differ, characteristic fractions from regenerating blood contained more alkali-labile phosphate than did their counterparts from normal blood. Furthermore, the phosphate content of the erythrocyte-specific component was appreciably greater than that of any other histone.The problem of distinguishing between contamination and valid histone phosphate is considered; complex formation between nuclear phosphoprotein and specific histone fractions could not be unequivocally eliminated. The pronounced phosphate levels in the erythrocyte-specific histone V are discussed in relation to the prospective roles of histone phosphorylation.

Genetic polymorphism of erythrocyte histone H1 in Japanese quail

“…The two-dimensional gel patterns of erythrocyte H1 from quail individuals differing in H1.3 phenotype clearly demonstrate that each exhibits just one or both types of polypeptides: Hl.bl and/or Hl.b2. Moreover, the level of phosphorylated H1 molecules is very low in mature erythrocytes (Adams et al, 1970). 1, right) has a similar molecular weight (Fig.…”

A Study of the Quantitative Variation of Histones, and Their Relationship to RNA Synthesis, during Erythropoiesis in the Adult Chicken

“…Sadgopal and Kabat [46] have claimed that only arginine-rich histones (F3 + 2al) are synthesised in cell populations from anaemic chicken blood. However, the method used by these authors to fractionate histones (chromatography on Amberlite ion-exchange resin) does not separate F2c from F3 + 2ai L14,47], so that their results may reflect a synthesis of F2c Indeed, Adams et al [48] report that lysine is incorporated into F2c more rapidly than into other histone fractions, in anaemic erythrocyte populations. Although no synthetic studies have been included in the present investigation, clearly activation of the gene(s) coding for FZc, and initiation of synthesis of F2c must occur a t a very early stage of erythropoiesis, i.e.…”

“…I n fact, Adams et aE. [48] have produced evidence that the phosphate content of F2c decreases during final stages of erythrocyte muturation. A decrease in non-histone protein and RNA content of erythrocyte chromatin during final maturation has been reported [lo, 531 ; some of the slowly migrating non-histone bands observed in Fig.…”

Histones and Nucleohistones

“…The major product of the reaction is O-phosphoserine [317,318], which occurs at a single specific residue in the histone molecule [148,319,331]. Histones other than Fl(I), including F2B(I1b2) and F3(I1I), also appear to be phosphorylated [245,280,316,317,320,321,333,334]. The reaction has been studied in isolated nuclei [317,322], and in cell-free enzyme systems from various sources [319,323,324,325,327,329,331].…”