TABLE 3.
Oligopeptide composition of the C. elegans linker histonesa
| Peptide | No. of occurrences in:
|
|||||||
|---|---|---|---|---|---|---|---|---|
| H1.1 | H1.2 | H1.3 | H1.4 | H1.5 | H1.6 | H1.Q | H1.X | |
| AAAKKP | 3 | 0 | 1 | 0 | 0 | 0 | 0 | 0 |
| PAAAKK | 3 | 0 | 0 | 1 | 0 | 0 | 0 | 0 |
| PAAAKKP | 2 | 0 | 0 | 0 | 0 | 0 | 0 | 0 |
| AAAKK | 4 | 0 | 1 | 1 | 0 | 0 | 1 | 0 |
| AAKK | 6 | 1 | 1 | 1 | 0 | 1 | 1 | 0 |
a
H1.1 contains 35% more alanine residues than the remaining canonical linker histones of C. elegans. The additional alanine residues are located in the first half of the C-terminal domain, where they contribute to a repeated oligopeptide structure. The numbers of occurrences of different possible overlapping versions of this oligopeptide are presented. All indicated peptides are repeated in H1.1, but they are unique or absent in the remaining proteins.