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Four domains of Ada1 form a heterochromatin boundary through different mechanisms
Author(s) -
Kamata Kazuma,
Shinmyozu Kaori,
Nakayama Junichi,
Hatashita Masanori,
Uchida Hiroyuki,
Oki Masaya
Publication year - 2016
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12421
Subject(s) - biology , chromatin , histone , microbiology and biotechnology , proteasome , function (biology) , gene , genetics
In eukaryotic cells, there are two chromatin states, silenced and active, and the formation of a so‐called boundary plays a critical role in demarcating these regions; however, the mechanisms underlying boundary formation are not well understood. In this study, we focused on S. cerevisiae ADA 1 , a gene previously shown to encode a protein with a robust boundary function. Ada1 is a component of the histone modification complex Spt–Ada–Gcn5–acetyltransferase ( SAGA ) and the SAGA ‐like ( SLIK ) complex, and it helps to maintain the integrity of these complexes. Domain analysis showed that four relatively small regions of Ada1 (Region I; 66–75 aa, II ; 232–282 aa, III ; 416–436 aa and IV ; 476–488 aa) have a boundary function. Among these, Region II could form an intact SAGA complex, whereas the other regions could not. Investigation of cellular factors that interact with these small regions identified a number of proteasome‐associated proteins. Interestingly, the boundary functions of Region II and Region III were affected by depletion of Ump1, a maturation and assembly factor of the 20S proteasome. These results suggest that the boundary function of Ada1 is functionally linked to proteasome processes and that the four relatively small regions in ADA 1 form a boundary via different mechanisms.