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The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing [RNA-seq]

ABSTRACT: The mechanism by which MORPHEUS'MOLECULE1 (MOM1) contributes to transcriptional gene silencing remained elusive since the gene was first identified and characterized (Amedeo et al., 2000). Here, we report that two PIAS (PROTEIN INHIBITOR OF ACTIVATED STAT)-type SUMO E3 ligase-like proteins PIAL1 and PIAL2 function redundantly to mediate transcriptional silencing at MOM1 target loci. PIAL1 and PIAL2 physically interact with each other and with MOM1 to form a high-molecular-weight complex. In the absence of either PIAL2 or MOM1, the formation of the high-molecular-weight complex was disrupted. We identified a previously uncharacterized IND (interacting domain) in PIAL1 and PIAL2, and demonstrated that IND directly interacts with MOM1. The CMM2 (conserved MOM1 motif 2) domain of MOM1 was previously shown to be required for the dimerization of MOM1. We demonstrated that the CMM2 domain is also required for the interaction of MOM1 with PIAL1 and PIAL2. We found that although PIAL2 has a SUMO E3 ligase activity, the activity is dispensable for PIAL2 in transcriptional silencing. This study suggests that PIAL1 and PIAl2 act as components of the MOM1-containing complex to mediate transcriptional silencing at heterochromatin regions.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE80301 | GEO | 2016/04/15

SECONDARY ACCESSION(S): PRJNA318519

REPOSITORIES: GEO

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The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing [Bisulfite-seq]

Project description:The mechanism by which MORPHEUS'MOLECULE1 (MOM1) contributes to transcriptional gene silencing remained elusive since the gene was first identified and characterized (Amedeo et al., 2000). Here, we report that two PIAS (PROTEIN INHIBITOR OF ACTIVATED STAT)-type SUMO E3 ligase-like proteins PIAL1 and PIAL2 function redundantly to mediate transcriptional silencing at MOM1 target loci. PIAL1 and PIAL2 physically interact with each other and with MOM1 to form a high-molecular-weight complex. In the absence of either PIAL2 or MOM1, the formation of the high-molecular-weight complex was disrupted. We identified a previously uncharacterized IND (interacting domain) in PIAL1 and PIAL2, and demonstrated that IND directly interacts with MOM1. The CMM2 (conserved MOM1 motif 2) domain of MOM1 was previously shown to be required for the dimerization of MOM1. We demonstrated that the CMM2 domain is also required for the interaction of MOM1 with PIAL1 and PIAL2. We found that although PIAL2 has a SUMO E3 ligase activity, the activity is dispensable for PIAL2 in transcriptional silencing. This study suggests that PIAL1 and PIAl2 act as components of the MOM1-containing complex to mediate transcriptional silencing at heterochromatin regions.

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The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing

Project description:The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing

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The MOM1 complex recruits the RdDM machinery via MORC6 to establish de novo DNA methylation.

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