Calf Thymus Lysine- and Serine-rich Histone

Iwai, Koichi; Hayashi, Hiroaki; Ishikawa, Katsutoshi

doi:10.1093/oxfordjournals.jbchem.a129911

Cited by 80 publications

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“…5 ) onwards has been conserved. This region has remained virtually unchanged when calf thymus H2B [34] is compared to the sea urchin proteins [32]. Certain changes at various positions in this otherwise conservative part of the protein do, however, occur.…”

Section: Discussionmentioning

confidence: 96%

“…A number of variants of histones H2B had been isolated previously from sperm cells of various species of sea urchin : Purrchinus ungulosus [ 1,2 1, Psarnrnechinus rniliaris [32] and Echinolumpus crassa (our unpublished results). All of these sperm histones H2B show an elongation of the amino-terminal region when compared to the histone H2BCalf [34]. These extensions contain a variable number of different repeating amino acid sequences.…”

Section: Discussionmentioning

confidence: 99%

“…5). Remnants of such a repetitive structure can also be seen in the somatic histones H2B from bovine thymus [34] and the erythrocytes of Gallus ciomesticus, Xenopirs Iwvis and Crocodilus niloticus [38] namely, residues 3 -7 and 10 -14. A similar pentapeptide repeat is also found in histone H2B from trout testes from residues 3 -7 and 8-12 [39].…”

Section: Discussionmentioning

confidence: 99%

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The Complete Amino‐Acid Sequence of Histone H2B₍₃₎ from Sperm of the Sea Urchin Parechinus angulosus

Strickland

Brandt

et al. 1978

European Journal of Biochemistry

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The primary structure of a third H2B histone isolated from sperm of the sea urchin Parechinus angulosus has been determined. H2B(3, consists of a polypeptide chain of the following 148 amino acid residue5 : Pro-Arg-Ser-Pro- A third protein has now been identified in the complement of H2B histones of animals of the same sea urchin species. The amino acid sequence of this histone H2B(3) Parerhinus is reported. MATERIALS AND METHODS Purification of HistonesHistone H2B(3) was purified by selective extraction [3], gel exclusion chromatography on Biogel P60, and ion-exchange chromatography on carboxymethyl-cellulose (CM-cellulose) as previously described for the other histone H2B variants. The yields from 100 g wet packed sperm were: 0.7 g (histone H1) in the perchloric acid extract, 1.7 g (histones H4, H3, H2A) in the 80% ethanol/0.25 M HC1 extract and 1.0 g (histone H2B, H1 and non-histone proteins) in the 0.25 M HCl extract; about 0.5 g of H2B mixture (Fig. 1) was obtained from the 0.25 M HCl extract after Biogel P60 fractionation. The yield of histone H2B was 14.7% of the total histones extracted. The yield of histone H2B variants from a typical CMcellulose run is shown in Fig. 2 B.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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The Complete Amino‐Acid Sequence of Histone H2B₍₃₎ from Sperm of the Sea Urchin Parechinus angulosus

Strickland

Brandt

et al. 1978

European Journal of Biochemistry

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“…There are also three lysine to arginine substitutions in the relatively constant carboxyl-terminal halves to these two proteins and in all cases of lysinei arginine substitution arginine occurs in sea urchin whereas lysine occurs in calf. The remainder of the H2B(1) molecule from residue 54 to the carboxyl terminal end is almost identical to the corresponding regions of calf H2B [5,26]. There is one polar region between residues 95 and 114 where there are seven variable residues.…”

Section: Discussionmentioning

confidence: 89%

“…In common with calf thymus H2B [5,25] the amino-terminal region is highly basic. However, in H2B(1, of sea urchin the amino-terminal region shows an extension of 19 amino acids beyond the amino-terminal proline residue of calf H2B.…”

Section: Discussionmentioning

confidence: 99%

The Complete Amino‐Acid Sequence of Histone H2B₍₁₎ from Sperm of the Sea Urchin Parechinus angulosus

Strickland

Brandt

et al. 1977

European Journal of Biochemistry

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Two histones have been isolated and purified from sperm cells of the sea urchin Parechinus angularus. They have been designated sperm histone H2B(1)1+,~~.~hi~~~ and sperm histone H2B~)~aveehinus on criteria of solubility and partial sequence homology with H2BCalf.H2B (1) consists of a polypeptide chain of the following 144 amino acid residues: Pro-Ser-GlnLys-Ser-Pro-Thr-Lys-Arg-Ser-Pro-Thr-Lys-Arg-Ser-Pro-Thr-Lys-Arg-Ser-Pro-Gln-Lys-Gly Gly-Lys-Gly-Gly-Lys-Gly-Ala-Lys-Arg-Gly-Gly-Lys-Ala-Gly-Lys-Arg-Arg-Arg-Gly-Val-GlIn a previously published partial sequence serine was incorrectly assigned to position 30. A comparison of the carboxyl-terminal two thirds of H2B(1)parechinus and H2B,,lf reveals that 79 of the corresponding positions are occupied by identical amino acid residues. Much of the variability occurs in a short polar region of 20 amino acid residues. The remainder of C-terminal regions is hydrophobic and almost completely invariable.A comparison of the amino-terminal one third of H~B ( I ) P~~~,~~~~~~~ and H2B,,lc reveals that they are both highly basic with a considerable homology of the position of basic amino acids. Further, H2B(1)pavec,,inus possesses an amino terminal extension of 19 amino acids. These 19 amino acids can be recognized as a repeating pentapeptide.Five major species of histones have been recognized in calf thymus chromatin and their primary structures have been determined. These five histones have been described in other species as well and in a number of cases, the primary structures have been partially or completely determined. From these investigations it appears that the sequences of histones H3 and H4 are extremely conservative over a wide spectrum of the biological world [l], while that of HI is quite variable even between the HI histones isolated from different tissues of the same organism Ahhreviation. Dansyl, 5-dimethylaminonaphthalonesulfonyl. [2,3]. Histones H2A and H2B appear to be intermediate in variability [4-81. We have previously extracted two proteins from sperm of the sea urchin ParechinuJ angulosus that we classified by solubility criteria as H2B [9]. Partial sequence of these two proteins indicated a close homogology to calf thymus H2B at the carboxyl end. The N-terminal sequences, however, of the two proteins not only differed considerably from each other but showed little homology to calf thymus histone H2B. Nevertheless, these two sea urchin proteins were sub-classified as H2B(1) and H2B(2, on the strength of their solubility criteria and C-terminal sequence homologies. In this paper the complete amino acid sequence of sea urchin sperm histone H2B(1) is described, while the following paper presents the complete amino acid sequence of sea urchin hist one H 2B ( 2 ) .

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Histone Function and Evolution as Viewed by Sequence Studies

DeLange

Smith

1975

Novartis Foundation Symposia

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Calf Thymus Lysine- and Serine-rich Histone

Cited by 80 publications

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The Complete Amino‐Acid Sequence of Histone H2B₍₃₎ from Sperm of the Sea Urchin Parechinus angulosus

The Complete Amino‐Acid Sequence of Histone H2B₍₃₎ from Sperm of the Sea Urchin Parechinus angulosus

The Complete Amino‐Acid Sequence of Histone H2B₍₁₎ from Sperm of the Sea Urchin Parechinus angulosus

Histone Function and Evolution as Viewed by Sequence Studies

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Calf Thymus Lysine- and Serine-rich Histone

Cited by 80 publications

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The Complete Amino‐Acid Sequence of Histone H2B(3) from Sperm of the Sea Urchin Parechinus angulosus

The Complete Amino‐Acid Sequence of Histone H2B(3) from Sperm of the Sea Urchin Parechinus angulosus

The Complete Amino‐Acid Sequence of Histone H2B(1) from Sperm of the Sea Urchin Parechinus angulosus

Histone Function and Evolution as Viewed by Sequence Studies

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The Complete Amino‐Acid Sequence of Histone H2B₍₃₎ from Sperm of the Sea Urchin Parechinus angulosus

The Complete Amino‐Acid Sequence of Histone H2B₍₃₎ from Sperm of the Sea Urchin Parechinus angulosus

The Complete Amino‐Acid Sequence of Histone H2B₍₁₎ from Sperm of the Sea Urchin Parechinus angulosus