F2 Structure Research Articles

Behaviour of tyrosyl residues of calf-thymus histone F3. Difference-spectroscopy studies.

We have studied the behaviour of microenvironments containing tyrosine of calf thymus histone F3 (or histone H3) by using the difference spectroscopy techniques of thermal and solvent perturbation. By comparison of the parameters found for the models L-tyrosine methyl ester and N-acetyl-L-tyrosine ethyl ester with those for the protein at various conditions, several aspects of the tertiary structure of histone F3 become apparent. The raising of ionic strength produces a general burial of tyrosyl residues of the histone, whereas low pH or urea treatment causes a complete exposure of tyrosyl groups with respect to the solvent. Anomalously high values can also be observed of accessibility of the perturbants sucrose and ethylene glycol at low concentrations of phosphate buffer. The relevance of these findings towards a better understanding of the tertiary structure of histone F3 and of its interactions with DNA is discussed.

The determination of the primary structure of histones F3 from chicken erythrocytes by automatic Edman degradation. 1. Cleavage and alignment of fragments.

In order to determine the sequence of histone F3 by automatic Edman degradation, this protein was fragmented into a series of smaller fragments. Specific chemical cleavages rather than enzymatic degradations were applied in such a way as to yield a limited number of larger fragments.In the first step the histone F3 dimer was cleaved at the two methionine residues with cyanogen bromide. The three fragments were separated and purified by gel filtration. Their respective sizes were 90, 30 and 15 amino‐acid residues.The two larger fragments were both cleaved with N‐bromosuccinimide at tyrosine residues. They in turn yielded three and two fragments, respectively, which could be readily purified by gel filtration and carboxymethyl‐cellulose ion‐exchange chromatography.One of the larger fragments obtained by cleaving the 90 residue fragment at its tyrosine residues was further degraded by dilute acid into another three fragments and two free aspartic acid residues which also could be purified by gel filtration.The position of all the 10 fragments in the protein molecule became apparent by comparing the N‐ and C‐terminal amino‐acid residues of the starting material and the cleaved products after each cleavage.The simplicity of the peptide mixture after each cleavage resulted in an easy separation of the fragments.

The determination of the primary structure of histone F3 from chicken erythrocytes by automatic Edman degradation. 2. Sequence analysis of histone F3.

Histone F3 has been fragmented into 10 non‐overlapping fragments.With the aid of the automatic Edman degradation procedure for proteins using 3‐(N,N‐dimethylamino)propyne buffer the first 48 amino‐acid residues in the uncleaved protein have been positioned.The remainder of the amino‐acid sequence of this protein was elucidated by subjecting the aligned peptides to the automatic degradation. The amino acids obtained during the degradation were quantitated and identified by gas chromatography and amino‐acid analysis.The primary structure of this histone is compared to the corresponding fraction from calf which had been independently determined by another laboratory.

The primary structure of histone F3 from shark erythrocytes

FEBS LettersVolume 40, Issue 2 p. 349-352 Full-length articleFree Access The primary structure of histone F3 from shark erythrocytes W.F. Brandt, W.F. Brandt Department of Biochemistry, University of Cape Town, Rondebosch 7700, South AfricaSearch for more papers by this authorW.N. Strickland, W.N. Strickland Department of Biochemistry, University of Cape Town, Rondebosch 7700, South AfricaSearch for more papers by this authorC. Von Holt, C. Von Holt Department of Biochemistry, University of Cape Town, Rondebosch 7700, South AfricaSearch for more papers by this author W.F. Brandt, W.F. Brandt Department of Biochemistry, University of Cape Town, Rondebosch 7700, South AfricaSearch for more papers by this authorW.N. Strickland, W.N. Strickland Department of Biochemistry, University of Cape Town, Rondebosch 7700, South AfricaSearch for more papers by this authorC. Von Holt, C. Von Holt Department of Biochemistry, University of Cape Town, Rondebosch 7700, South AfricaSearch for more papers by this author First published: April 01, 1974 https://doi.org/10.1016/0014-5793(74)80261-9Citations: 19AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume40, Issue2April 01, 1974Pages 349-352 ReferencesRelatedInformation