Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing.
Increasing evidence suggests that chromatin modifications have important roles in modulating constitutive or alternative splicing. Here we demonstrate that the PWWP domain of the chromatin-associated protein Psip1/Ledgf can specifically recognize tri-methylated H3K36 and that, like this histone modi...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2012-01-01
|
| Series: | PLoS Genetics |
| Online Access: | http://europepmc.org/articles/PMC3355077?pdf=render |
| _version_ | 1818335621832245248 |
|---|---|
| author | Madapura M Pradeepa Heidi G Sutherland Jernej Ule Graeme R Grimes Wendy A Bickmore |
| author_facet | Madapura M Pradeepa Heidi G Sutherland Jernej Ule Graeme R Grimes Wendy A Bickmore |
| author_sort | Madapura M Pradeepa |
| collection | DOAJ |
| description | Increasing evidence suggests that chromatin modifications have important roles in modulating constitutive or alternative splicing. Here we demonstrate that the PWWP domain of the chromatin-associated protein Psip1/Ledgf can specifically recognize tri-methylated H3K36 and that, like this histone modification, the Psip1 short (p52) isoform is enriched at active genes. We show that the p52, but not the long (p75), isoform of Psip1 co-localizes and interacts with Srsf1 and other proteins involved in mRNA processing. The level of H3K36me3 associated Srsf1 is reduced in Psip1 mutant cells and alternative splicing of specific genes is affected. Moreover, we show altered Srsf1 distribution around the alternatively spliced exons of these genes in Psip1 null cells. We propose that Psip1/p52, through its binding to both chromatin and splicing factors, might act to modulate splicing. |
| first_indexed | 2024-12-13T14:26:21Z |
| format | Article |
| id | doaj.art-caf1e9bc2b614e498b20e6d42f75bb22 |
| institution | Directory Open Access Journal |
| issn | 1553-7390 1553-7404 |
| language | English |
| last_indexed | 2024-12-13T14:26:21Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Genetics |
| spelling | doaj.art-caf1e9bc2b614e498b20e6d42f75bb222022-12-21T23:41:56ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042012-01-0185e100271710.1371/journal.pgen.1002717Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing.Madapura M PradeepaHeidi G SutherlandJernej UleGraeme R GrimesWendy A BickmoreIncreasing evidence suggests that chromatin modifications have important roles in modulating constitutive or alternative splicing. Here we demonstrate that the PWWP domain of the chromatin-associated protein Psip1/Ledgf can specifically recognize tri-methylated H3K36 and that, like this histone modification, the Psip1 short (p52) isoform is enriched at active genes. We show that the p52, but not the long (p75), isoform of Psip1 co-localizes and interacts with Srsf1 and other proteins involved in mRNA processing. The level of H3K36me3 associated Srsf1 is reduced in Psip1 mutant cells and alternative splicing of specific genes is affected. Moreover, we show altered Srsf1 distribution around the alternatively spliced exons of these genes in Psip1 null cells. We propose that Psip1/p52, through its binding to both chromatin and splicing factors, might act to modulate splicing.http://europepmc.org/articles/PMC3355077?pdf=render |
| spellingShingle | Madapura M Pradeepa Heidi G Sutherland Jernej Ule Graeme R Grimes Wendy A Bickmore Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. PLoS Genetics |
| title | Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. |
| title_full | Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. |
| title_fullStr | Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. |
| title_full_unstemmed | Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. |
| title_short | Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing. |
| title_sort | psip1 ledgf p52 binds methylated histone h3k36 and splicing factors and contributes to the regulation of alternative splicing |
| url | http://europepmc.org/articles/PMC3355077?pdf=render |
| work_keys_str_mv | AT madapurampradeepa psip1ledgfp52bindsmethylatedhistoneh3k36andsplicingfactorsandcontributestotheregulationofalternativesplicing AT heidigsutherland psip1ledgfp52bindsmethylatedhistoneh3k36andsplicingfactorsandcontributestotheregulationofalternativesplicing AT jernejule psip1ledgfp52bindsmethylatedhistoneh3k36andsplicingfactorsandcontributestotheregulationofalternativesplicing AT graemergrimes psip1ledgfp52bindsmethylatedhistoneh3k36andsplicingfactorsandcontributestotheregulationofalternativesplicing AT wendyabickmore psip1ledgfp52bindsmethylatedhistoneh3k36andsplicingfactorsandcontributestotheregulationofalternativesplicing |