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KMID : 0364820170530040286
Korean Journal of Microbiology
2017 Volume.53 No. 4 p.286 ~ p.291
The effect of Swd2¡¯s binding to Set1 on the dual functions of Swd2 in Saccharomyces cerevisiae
Park Shin-Ae

Lee Jung-Shin
Abstract
In eukaryotic cells, histone modification is an important mechanism to regulate the chromatin structure. The methylation of the fourth lysine on histone H3 (H3K4) by Set1 complex is one of the various well-known histone modifications. Set1 complex has seven subunits including Swd2, which is known to be important for H2B ubiquitination dependent on H3K4 methylation. Swd2 was reported to regulate Set1¡¯s methyltransferase activity by binding to near RNA recognition motif (RRM) domain of Set1 and to act as a component of CPF (Cleavage and Polyadenylation Factors) complex involved in RNA 3¡¯ end processing. According to the recent reports, two functions of Swd2 work independently of each other and the lethality of Swd2 knockout strain was known to be caused by its function as a component of CPF complex. In this study, we found that Swd2 could influence the Set1¡¯s stability as well as histone methyltransferase activity through the association with RRM domain of Set1. Also, we found that ¡âswd2 mutant bearing truncated-Set1, which cannot interact with Swd2, lost its lethality and grew normally. These results suggest that the dual functions of Swd2 in H3K4 methylation and RNA 3¡¯ end processing are not independent in Saccharomyces cerevisiae.
KEYWORD
Saccharomyces cerevisiae, CPF complex, histone H3K4 methylation, Set1, Swd2
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