Abstract:
:The abundant heterogeneous nuclear ribonucleoprotein M (hnRNP M) is able to associate with early spliceosomes and to influence splicing patterns of specific pre-mRNAs. Here, by a combination of immunoprecipitation and pull-down assays, we have identified PSF (polypyrimidine tract-binding protein-associated splicing factor) and p54(nrb), two highly related proteins involved in transcription and RNA processing, as new binding partners of hnRNP M. HnRNP M was found to co-localize with PSF within a subset of nuclear paraspeckles and to largely co-fractionate with PSF and p54(nrb) in biochemical nuclear matrix preparations. In cells transfected with an alternatively spliced preprotachykinin (PPT) minigene expression of hnRNP M promoted exon skipping while expression of PSF favours exon inclusion. The latter effect was reverted specifically by co-expressing the full length hnRNP M or a deletion mutant capable of interaction with PSF and p54(nrb). Together our data provide new insights and some functional implications on the hnRNP M network of interactions.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Marko M,Leichter M,Patrinou-Georgoula M,Guialis Adoi
10.1016/j.yexcr.2009.10.021subject
Has Abstractpub_date
2010-02-01 00:00:00pages
390-400issue
3eissn
0014-4827issn
1090-2422pii
S0014-4827(09)00461-3journal_volume
316pub_type
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