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5198597 
Journal Article 
Structural properties of the methionine-containing subfraction of rat liver histone H1 
Mitchell, TC; Sautiere, P; Turner, C; Böhm, L 
1985 
1 
Biochimica et Biophysica Acta
ISSN: 0006-3002
EISSN: 1878-2434 
832 
3 
235-241 
English 
4074746 
Cyanogen bromide (CNBr) cleavage of total rat liver histone H1 generates a C-terminal peptide which originates from a methionine-containing subfraction. This subfraction comprises approx. 20% of the whole rat liver H1 population, resembles calf thymus CTL-1 in size but contains methionine and histidine, higher proportions of serine and less alanine and proline. Edman degradation established the N-terminal sequence of the CNBr peptide as Arg-Arg-Lys-Ala-Ser-Gly-Pro-Pro-Val-Glu. By alignment with calf thymus CTL-1, methionine was identified as residue 30 replacing alanine in a non-conservative replacement. Residue 40 is deleted but sequence homology near the double proline sequence in the G-domain is retained. The CNBr peptide is estimated at 177-181 residues and comprises the complete G- and C-domain and two arginines from the basic cluster in the N-domain. Removal from H1 of all but two residues of the N-domain does not abolish secondary and tertiary folding. This GC-peptide opens new approaches to the study of the function of H1 in chromatin.