MBE Advance Access published online on March 5, 2003
Molecular Biology and Evolution, doi:10.1093/molbev/msg041
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2003; all rights reserved
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1 Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Autónoma de Barcelona, 08193 Bellaterra, Barcelona, Spain
* To whom correspondence should be addressed. E-mail: Pere.Suau{at}uab.es.
H1 subtypes are involved in chromatin higher-order structure and gene regulation. H1 has a characteristic three-domain structure. We studied the length variation of the available H1 subtypes and showed that the length of the N- and C-terminal domains was more variable than that of the central domain. The N- and C-terminal domains were of low sequence complexity, both at the nucleotide and the amino acid level, while the globular domain was of high complexity. In most subtypes, low complexity was due only to cryptic simplicity, which reflects the clustering of a number of short and often imperfect sequence motifs. However, a subset of subtypes from eubacteria, plants and invertebrates contained tandem repeats of short amino acid motifs (4-12 residues), which could amount to a large proportion of the terminal domains. In addition, some other subtypes, such as those of Drosophila and mammalian H1t, were only marginally simple. The coexistence of these three kinds of subtypes suggests that the terminal domains could have originated in the amplification of short sequence motifs, which would then have evolved by point mutation and further slippage. Key Words:
Histone H1, Simplicity, Slippage, Tandem repeats, Length mutations
© 2003 Society for Molecular Biology and Evolution
Original Articles
Sequence Complexity of Histone H1 Subtypes
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