Human Spleen Histone HI. Isolation and Amino Acid Sequence of a Main Variant, H1b1

Abstract

The complete amino acid sequence of a main variant, H1b, of human spleen histone H1 was determined, following previous determinations of human spleen histones H2B, H2A, H3, and H4. High-performance liquid chromatography on C8 silica of the H1 fraction yielded the homogeneous H1b subfraction; this variant was estimated to account for 60% of the total of the four H1 variants. The sequence determination was performed with four main fragments, I to IV, obtained by limited chymotryptic digestion of H1b. Together with direct sequencing by automated Edman degradation of fragments II, III, and IV, fragment I, blocked at the N-terminal, and fragment IV, the C-terminal half the H1b molecule, were sequenced after further digestion with staphylococcal protease and others. The four fragments were aligned with three overlapping peptides each derived from chymotryptic partial fragments, I-II and I-II-III, and intact H1b. Carboxypeptidase digestion of intact H1b confirmed the C-terminal sequence of the molecule. Thus, the total sequence of H1b was completely determined; it consists of a total of 218 amino acid residues, has a molecular weight of 21,734 in the unmodified form, and is completely acetylated at the N-terminal serine residue and partially methylated at the lysine residue 25. This sequence is compared with two mammalian somatic H1 sequences.

Characterization of the Mitotic Specific Phosphorylation Site of Histone H1

“…Sequence analysis demonstrated that the mitotic specific phosphorylation site of CHO H1 is on the end of the N-terminal tail and (Liao and Cole, 1981), rat liver (Cole et al, 1990), human spleen (Ohe et al, 1986(Ohe et al, , 1989, mouse (Yang et al, 1987), rabbit thymus (Rall and Cole 1971;Jones, et al, 1974), and human placenta (Parseghian et al, 1994) were compared with that from CHO (first line in panels B and C). In these comparisons the asterisk indicates that the amino acid in that position is the same as that in CHO H1.…”

Linker histone‐DNA complexes: enhanced stability in the presence of aluminum lactate and implications for Alzheimer's disease

“…In the present paper we have examined the binding of human linker histones Hlb, Hla and H1 ° [10,12,13] to a human 300 base pair (bp) double-stranded Alu repetitive element [14,15] utilizing a mobility shift assay [16,17]. Discrete DNP species were analyzed through integration in-to a TGSDS-PAGE system to ascertain the type of interacting protein species [4].…”

The b mating-type locus of Ustilago maydis contains variable and constant regions.

“…4A; Danielsen et al 1986;Guiochon-Mantel et al 1989} and to histone genes ( Fig. 4B; Ohe et al 1986}. This region also contains a motif similar to that described by Dingwall et al (1989) for nuclear localization sequences; that is, a periodic motif with three basic tracts separated by two sequences of four hydrophobic residues.…”

“…A potential nuclear localization sequence in the bl polypeptide. The amino acid sequence (one letter code) of the bl polypeptide between residues 276 and 308 is aligned with a similar region from (A) the mouse glucocorticoid receptor (Danielsen et al 1986) and (B) two histone genes (Wallis et al 1980;Ohe et al 1986). The region shown for the glucocorticoid receptor is believed to play a role in nuclear localization (Guiochon-Mantel et al 1989).…”