Mammalian splicing factor SF1 interacts with SURP domains of U2 
snRNP-associated proteins.

Crisci, C.; Raleff, F.; Bagdul, I.; Raabe, M.; Urlaub, H.; Rain, J. C.; Krämer, A.

doi:10.1093/nar/gkv952

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.

MPS-Authors

/persons/resource/persons15676

Raabe, M.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub, H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

External Resource

http://nar.oxfordjournals.org/content/43/21/10456.full.pdf+html
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

2235402.pdf
(Publisher version), 6MB

Supplementary Material (public)

2235402_Suppl_1.pdf
(Supplementary material), 661KB

2235402_Suppl_2.pdf
(Supplementary material), 5MB

2235402_Suppl_3.pdf
(Supplementary material), 71KB

2235402_Suppl_4.xlsx
(Supplementary material), 110KB

Citation

Crisci, C., Raleff, F., Bagdul, I., Raabe, M., Urlaub, H., Rain, J. C., et al. (2015). Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins. Nucleic Acids Research, 43(21), 10456-10473. doi:10.1093/nar/gkv952.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-272F-1

Abstract

Splicing factor 1 (SF1) recognizes the branch point sequence (BPS) at the 3' splice site during the formation of early complex E, thereby pre-bulging the BPS adenosine, thought to facilitate subsequent base-pairing of the U2 snRNA with the BPS. The 65-kDa subunit of U2 snRNP auxiliary factor (U2AF65) interacts with SF1 and was shown to recruit the U2 snRNP to the spliceosome. Co-immunoprecipitation experiments of SF1-interacting proteins from HeLa cell extracts shown here are consistent with the presence of SF1 in early splicing complexes. Surprisingly almost all U2 snRNP proteins were found associated with SF1. Yeast two-hybrid screens identified two SURP domain-containing U2 snRNP proteins as partners of SF1. A short, evolutionarily conserved region of SF1 interacts with the SURP domains, stressing their role in protein-protein interactions. A reduction of A complex formation in SF1-depleted extracts could be rescued with recombinant SF1 containing the SURP-interaction domain, but only partial rescue was observed with SF1 lacking this sequence. Thus, SF1 can initially recruit the U2 snRNP to the spliceosome during E complex formation, whereas U2AF65 may stabilize the association of the U2 snRNP with the spliceosome at later times. In addition, these findings may have implications for alternative splicing decisions.