SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus.
Histone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors is regulated by enzymes that acetylate and deacetylate histones. The Sin3A corepressor complex recruits histone deacetylases and in many cases represses transcription. Here, we report that SAP30L, a close homolog of Sin3-associated protein 30 (SAP30), interacts with several components of the Sin3A corepressor complex. We show that it binds to the PAH3/HID (Paired Amphipathic Helix 3/Histone deacetylase Interacting Domain) region of mouse Sin3A with residues 120-140 in the C-terminal part of the protein. We provide evidence that SAP30L induces transcriptional repression, possibly via recruitment of Sin3A and histone deacetylases. Finally, we characterize a functional nucleolar localization signal in SAP30L and show that SAP30L and SAP30 are able to target Sin3A to the nucleolus.
Viiri
K M
KM
Paediatric Research Centre, University of Tampere Medical School and Tampere University Hospital, Tampere, Finland.
Korkeamäki
H
H
Kukkonen
M K
MK
Nieminen
L K
LK
Lindfors
K
K
Peterson
P
P
Mäki
M
M
Kainulainen
H
H
Lohi
O
O
D000818:Animals; D002460:Cell Line; D002466:Cell Nucleolus / Q000737:chemistry / Q000378:metabolism*; D020868:Gene Silencing; D006655:Histone Deacetylases / Q000378:metabolism; D006801:Humans; D051379:Mice; D009687:Nuclear Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D021382:Protein Sorting Signals; D021381:Protein Transport; D012097:Repressor Proteins / Q000378:metabolism*; D056264:Sin3 Histone Deacetylase and Corepressor Complex
D009687:Nuclear Proteins; D021382:Protein Sorting Signals; D012097:Repressor Proteins; C113294:SAP30 protein, human; C487046:SAP30L protein, human; C099683:SIN3A transcription factor; D006655:Histone Deacetylases; D056264:Sin3 Histone Deacetylase and Corepressor Complex