Species and tissue specificity of very lysine-rich and serine-rich histones

Nelson, Robert D.; Yunis, Jörge J.

doi:10.1016/0014-4827(69)90155-4

Cited by 56 publications

(4 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…As we will show later, at least one of these "extra" bands is also present in cultured cell histones for it becomes strongly iodinated under certain conditions. It is not clear which one of these FI histones, if any, should be designated F2c, similar to the serine, lysine-rich histone found in avian erythrocytes (Edwards and Hnilica, 1968;Nelson and Yunis, 1969).…”

Section: Resultsmentioning

confidence: 99%

Iodination of Xenopus laevis histone F2a1 in chromatin

Biroc¹,

Reeder²

1976

Biochemistry

View full text Add to dashboard Cite

The reaction of calf thymus and Xenopus laevis histones with radioactive iodine has been studied under various conditions that affect chromatin structure. All histones from both species contain at least one tyrosine residue and, in a denaturing solvent, all the the histones react with iodine. Histone F2a1 has been studied in detail. Calf thymus F2a1 is known to contain four tyrosyls and all four react with iodine. In high voltage paper electrophoresis, the tyrosine-containing peptides from calf co-migrate with those from Xenopus F2a1, suggesting that the amino acid sequence is strongly conserved between these two species. Therefore, the published calf thymus F2a1 sequence has been used to order the Xenopus F2a1 peptides within the molecules. When gently isolated native chromatin is iodinated in a low ionic strength medium 60% of the radioactivity in F2a1 is in tyrosyl 88, 30% in tyrosyl 51, and tyrosyl 72 and 98 have almost no radioactivity. Reagents which remove the protein from the DNA (2 M NaCl) or partially disrupt protein tertiary structure (5 M urea) increase the reactivity of each of the four tyrosyls five- to tenfold, suggesting that all four are protected about equally by the overall folding of the chromatin. Isolated F2a1 iodinated in the presence of 10 M urea shows uniform labeling in each of the four peptides, suggesting that tyrosyl 72 and 98 are afforded some protection solely by protein-protein interactions. The stepwise removal of histones in increasing NaCl concentrations differentially increases the availability of each F2a1 tyrosyl. The preferential exposure of tyrosyl 88 coincides with the removal of the majority of F1 histones at 0.5 M NaCl while the gradual and stepwise increase in reactivity of tyrosyl 51, 72, and 98 correlates with the gradual removal of histones other than F1. Radioactive iodination of chromatin has been shown to be a sensitive probe for detecting changes in the association state (or conformation) of histone F2a1.

show abstract

Section: Resultsmentioning

confidence: 99%

Iodination of Xenopus laevis histone F2a1 in chromatin

Biroc¹,

Reeder²

1976

Biochemistry

View full text Add to dashboard Cite

show abstract

“…The primary structures of some of the corresponding fractions of histones from different mammalian tissues appear very similar (Crampton et al, 1957); the sequence of histone F2al from pea buds and calf thymus differs in only two amino acids (DeLange et al, 1969). Some evidence exists for variations in the amounts of histone Fl (Stellwagen and Cole, 1969) and in the proportions of the subfractions of Fl in different tissues (Nelson and Yunis, 1969;Hohmann and Cole, 1969;. Generally, the total amount of histone, and the distribution of the different fractions, remains fairly constant, even though there are variations in the genetic activity of the chromatin (Comings, 1967;Dingman and Sporn, 1964).…”

Section: Introductionmentioning

confidence: 92%

Total Protein, Deoxyribonucleic Acid, Ribonucleic Acid, and Histone Content of Isolated Nuclei of Chicken Erythrocytes

Isaacks

Guerrero

1974

Poultry Science

View full text Add to dashboard Cite

Nuclei were isolated from erythroid cells of thirteen day chick embryos, eighteen day chick embryos, and hens; total protein, DNA, RNA, and histone contents were determined per nucleus. The average picogram quantities of total protein, DNA, RNA, and histone per nucleus from erythrocytes of the hen were 3.20, 2.05, 0.33, and 1.74, respectively. The results were the same in nuclei from the erythrocytes of the two ages of embryos except that the average total protein in nuclei from 18-day embryos was 2.64 picograms. ABSTRACTThe egg characteristics of shell thickness, specific gravity, egg weight, width/length ratio and tint of the brown shell eggs were regressed on the shell strength measurements of non-destructive deformation and breaking strength. Six commercially available laying strains (3 white egg and 3 brown egg) were used to determine differences between

show abstract

“…Si les erythrocytes nuclees possedent une fraction histonique F2c qui leur est specifique (Nelson et Yunis 1969) et si quelques tissus animaux ou vegetaux renferment des histones dont le pourcentage en acides amines acides, ou en leurs amides, est particulierement eleve (Johns 1964, Spelsberg et Sarkissian 1970, Dastugue et d. 1970, ceci ne parait pas remettre en question le caractere aspecifique des histones dont le role dans l'organisation structurale et dans la regulation du materiel genetique est universellement admis (Zubay 1964, Huang et Bonner 1962, Butler 1966, Tsanev et Sendov 1971.…”

Section: Introductionunclassified

Etude des proteines an cours de la germination des graiues: Isolement et analyse des histories de radis Par

Grellet¹,

Guitton²

1973

Physiologia Plantarum

View full text Add to dashboard Cite

Histones of radish seedlings have been characterised by comparison with pea histones extracted and purified under the same conditions. Submitted to acrylamide gel analysis the radish histones are resolved into main protein bands comparable to those of pea or calf thymus histones. However, protein bands of lesser importance which are not to be found in electrophoretic profils of pea or calf thymus histones, appear together with the main bands of radish histones. Study of these supplementary proteins through isoelectric focusing makes it possible to distinguish two groups: contaminating acid proteins and weakly basic proteins characterised by their high amide content.

show abstract

Species and tissue specificity of very lysine-rich and serine-rich histones

Cited by 56 publications

References 19 publications

Iodination of Xenopus laevis histone F2a1 in chromatin

Iodination of Xenopus laevis histone F2a1 in chromatin

Total Protein, Deoxyribonucleic Acid, Ribonucleic Acid, and Histone Content of Isolated Nuclei of Chicken Erythrocytes

Etude des proteines an cours de la germination des graiues: Isolement et analyse des histories de radis Par

Contact Info

Product

Resources

About