Document Detail

Alternative mRNA splicing of SAP30L regulates its transcriptional repression activity.
MedLine Citation:
PMID:  18070604     Owner:  NLM     Status:  MEDLINE    
Covalent modification of histones regulates chromatin structure and gene expression. Sin3A mediates the association of histone deacetylase enzymes with a large number of sequence-specific transcriptional repressors. In this study we characterized three novel transcripts of SAP30L, a recently identified Sin3A-associated protein. These splice variants show significant differences in transcriptional repression capabilities and associating histone deacetylase activities. Furthermore, they differ in binding to Sin3A and in subcellular localization when transiently transfected. These data suggest that the transcriptional repression of a Sin3A corepressor complex can be regulated not only by sequence-specific transcriptional repressors, but also by modification of associated proteins, such as SAP30L.
Hanna Korkeamäki; Keijo Viiri; Mari K Kukkonen; Markku Mäki; Olli Lohi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-12-10
Journal Detail:
Title:  FEBS letters     Volume:  582     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2008 Jan 
Date Detail:
Created Date:  2008-01-18     Completed Date:  2008-04-01     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  379-84     Citation Subset:  IM    
Paediatric Research Centre, University of Tampere Medical School, Tampere University Hospital, Tampere, Finland.
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MeSH Terms
Alternative Splicing*
Base Sequence
Cell Line
DNA Primers
DNA, Complementary
Gene Expression Regulation*
Histone Deacetylases / metabolism
Nuclear Proteins / genetics*
RNA, Messenger / metabolism*
Transcription, Genetic*
Reg. No./Substance:
0/DNA Primers; 0/DNA, Complementary; 0/Nuclear Proteins; 0/RNA, Messenger; 0/SAP30L protein, human; EC Deacetylases

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