Abstract
The chromatin organization of eukaryotic telomeres is essential for telomeric function and is currently receiving great attention. In yeast, the structural organization of telomeres involves a complex interplay of telomeric proteins that results in the formation of heterochromatin. This telomeric heterochromatin involves homotypic and heterotypic protein interactions that have been summarized in a general model. Recent analyses have focused on the study of the structural complexity at yeast telomeres to the level of specific nucleosomes and of the distribution of protein complexes in a natural telomeric region (LIII). In this report, we further analyze the structural complexity of LIII and the implication of this structure on telomeric silencing. It is shown that the establishment of repressive heterochromatin structures at LIII requires the recruitment of Sir3p through interaction with the N terminus of histone H4. The establishment of such structures does not require acetylation of any of four lysines located in the H4 N terminus (lysines 5, 8, 12, and 16).
Highlights
The chromatin organization of eukaryotic telomeres is essential for telomeric function and is currently receiving great attention
It is shown that the establishment of repressive heterochromatin structures at left arm of chromosome III (LIII) requires the recruitment of Sir3p through interaction with the N terminus of histone H4
We conclude that the establishment of repressive heterochromatin structures at LIII requires the recruitment of Sir3p through interaction with the N terminus of histone H4
Summary
RECRUITMENT OF Sir3p THROUGH INTERACTION WITH HISTONE H4 N TERMINUS IS REQUIRED FOR THE ESTABLISHMENT OF REPRESSIVE STRUCTURES*. Both the telosome and the X element are characterized by a tight chromatin structure organization. Sir3p is not required to keep the overall tight organization of the X element [21] This previous analysis of LIII has focused the study of the structural complexity at telomeres to the level of specific nucleosomes and of the distribution of protein complexes. It has provided in vivo evidence linking the modification of heterochromatin structure with the loss of transcriptional telomeric silencing [4]. The establishment of such structures does not require acetylation of any of the four lysines located in the H4 N terminus (lysines 5, 8, 12, and 16)
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