Amino-acid Sequence of Slightly Lysine-rich Histone

Iwai, Koichi; Ishikawa, Katsutoshi; Hayashi, Hiroaki

doi:10.1038/2261056b0

Cited by 167 publications

(45 citation statements)

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“…The (2) (1) (2) ( 1) ( 1) (1) 1.96 (2) 1.00( 3.14 (3) 0.92( 8.53 (9) Table 5. The complete amino acid sequence of histone H2B is known (Iwai et al, 1970) and inspection of the sequence allows the conclusion that the tryptiQ dipeptide T2 (Ser,Arg) is derived from the residues serine-32 and arginine-33. The amino acid composition of peptide Ti shows that this corresponds to residues 34-40, which have the sequence: Lys-Glu-Ser-Tyr-Ser-Val-Tyr.…”

Section: Resultsmentioning

confidence: 99%

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The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Yeaman¹,

Cohen²,

Watson³

et al. 1977

Biochemical Journal

144

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The known amino acid sequences at the two sites on phosphorylase kinase that are phosphorylated by cyclic AMP-dependent protein kinase were extended. The sequences of 42 amino acids around the phosphorylation site on the a-subunit and of 14 amino acids around the phosphorylation site on the fl.subunit were shown to be: a-subunit Phe-Arg-Arg-Leu-Ser(P)-I1e-Ser-Thr-Glu-Ser-Glx-Pro-Asx-Gly-Gly-His-Ser-Leu-GlyAla-Asp-Leu-Met-Ser-Pro-Ser-Phe-Leu-Ser-Pro-Gly-Th.r-Ser-Val-Phe(Ser,Pro,Gly)HisThr-Ser-Lys; 1)-subunit, Ala-Arg-Thr-Lys-Arg-Ser-Gly-Vr()alTyr-Glu-Pro-LeuLys. The sites on histone H2B which are phosphorylated by cyclic AMP-dependent protein kinase in vitro were identified as serine-36 and serine-32. The amino acid sequence 32 36 in this region is:

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Section: Resultsmentioning

confidence: 99%

“…in this region is: Lys-Lys-Arg-Lys-Arg-Ser(P)-Arg-Lys-Glu-Ser(P)-Tyr-Ser-Val-TyrVal-[lIwai, K., Ishikawa, K. & Hayashi, H. (1970) Nature (London) 226, 10561058]. was phosphorylated at 50% of the rate at which the f-subunit of phosphorylase kinase was phosphorylated, and it was phosphorylated 6-7-fold more rapidly than was serine-32.…”

mentioning

confidence: 99%

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Yeaman¹,

Cohen²,

Watson³

et al. 1977

Biochemical Journal

144

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“…This is probably a useful precaution to take in the case of other very basic proteins that are high in lysine content, since the e-amino groups of lysyl residues compete with the amino terminus of the protein for the phenylisothiocyanate reagent, until they become fully blocked by it. Thus, in the case of histone IIb2, there are about 20 e-amino groups (14) that can react with the Edman reagent in the first coupling step, and this competition for reagent could decrease the yield of the first residue because of incomplete coupling if the reagent is not in sufficiently great excess; this effect is particularly likely to occur when relatively large amounts of protein are used for sequencing.…”

Section: And 4)mentioning

confidence: 99%

Amino-Terminal Sequences and Sites of In Vivo Acetylation of Trout-Testis Histones III and IIb ₂

Candido

Dixon

1972

Proc. Natl. Acad. Sci. U.S.A.

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The sequences of the first 25 residues of histone III, and the first 22 residues of histone Ib2, from trout testis have been determined on an automatic protein sequencer. The amino-terminal sequence of trout-testis histone III is identical to the corresponding region of calfthymus histone III, whereas the trout-testis histone IIb2 sequence differs from that of calf-thymus histone 11b2 at several positions in the amino-terminal region. Several in vivo sites of acetylation of these trout-testis histones have also been determined, by the same automated procedure. In addition to the two main sites at lysyl residues 14 and 23 acetylated in calf-thymus histone III, a lower degree of acetylation at two other sites, lysyl residues 9 and 18, has been detected. Four sites of acetylation have also been detected in trout-testis histone IIb2, at lysyl residues 5, 10, 13, and 18. When the amino-acid sequences around the acetylated lysyl residues of different histones are compared, striking similarities are seen. The methods used in these studies should prove useful in elucidation of the locations of chemically stable modifications in other proteins.We have reported the locations of sites of acetylation in trouttestis histones IV and JIb1 (1, 2) by isolation and characterization of [14C]acetyl-labeled tryptic peptides. We also showed (2) that histones III and IIb2 were acetylated in trout testis. In histones IIb1 and IV, the amino-terminal residue is Nacetylserine, so that automatic sequential Edman degradation is impossible, but in the case of histones III and IIb2, the amino termini consist of unblocked alanyl and prolyl residues, respectively.In view of the placement of the two acetylated tryptic peptides-obtained by DeLange et al. (3) (2) on a 3 X 320-cm column of Bio-Gel P-10 eluted with 0.01 N HCl. Purity of the samples was monitored by electrophoresis on urea-aluminum lactate starch gels (6). The histone III used for sequencing experiments contained a mixture of the reduced (monomer) and oxidized (dimer) forms.Sequencing of Histones III and 11b2. The sample of histone, containing 0.5-1.2 uimol of protein, was dissolved in 0.6 ml of distilled water and placed in the reaction cup of a Beckman 890 protein sequencer. A program similar to that of Edman and Begg (7) or, in some cases, that of Niall et al. (8) was used. The 2-anilino-5-thiazolinone derivatives of the amino acids from the sequencer were converted to their more stable 3-phenyl-2-thiohydantoin (PTH) derivatives, as described by Edman and Begg (7), except that the 1 N HCl contained 1 mM ethanethiol. The PTH derivatives were then extracted from the HCl phases with ethyl acetate (2 X 0.7 ml, Reagent Grade). Arginine was detected either after acid hydrolysis of the HCl phase after conversion to its PTH derivative (7), or else PTH arginine was first extracted from the HCl phase with ethyl acetate, after neutralization of the HC1 with 1 M Na2HPO4. Amino acids were identified on a Beckman 120C amino-acid analyzer after hydrolysis of their PTH derivatives in 6 N ...

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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: 56%

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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Amino-acid Sequence of Slightly Lysine-rich Histone

Cited by 167 publications

References 21 publications

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Amino-Terminal Sequences and Sites of In Vivo Acetylation of Trout-Testis Histones III and IIb ₂

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

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Amino-acid Sequence of Slightly Lysine-rich Histone

Cited by 167 publications

References 21 publications

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Amino-Terminal Sequences and Sites of In Vivo Acetylation of Trout-Testis Histones III and IIb 2

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

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Amino-Terminal Sequences and Sites of In Vivo Acetylation of Trout-Testis Histones III and IIb ₂

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