English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

A new role for FBP21 as regulator of Brr2 helicase activity.

MPS-Authors
/persons/resource/persons188023

Lee,  C. T.
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;

Locator
There are no locators available
Fulltext (public)

2472401.pdf
(Publisher version), 4MB

Supplementary Material (public)

2472401_Suppl.pdf
(Supplementary material), 4MB

Citation

Henning, L. M., Santos, K. F., Sticht, J., Jehle, S., Lee, C. T., Wittwer, M., et al. (2017). A new role for FBP21 as regulator of Brr2 helicase activity. Nucleic Acids Research, 45(13), 7922-7937. doi:10.1093/nar/gkx535.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-CB96-1
Abstract
Splicing of eukaryotic pre-mRNA is carried out by the spliceosome, which assembles stepwise on each splicing substrate. This requires the concerted action of snRNPs and non-snRNP accessory proteins, the functions of which are often not well understood. Of special interest are B complex factors that enter the spliceosome prior to catalytic activation and may alter splicing kinetics and splice site selection. One of these proteins is FBP21, for which we identified several spliceosomal binding partners in a yeast-two-hybrid screen, among them the RNA helicase Brr2. Biochemical and biophysical analyses revealed that an intrinsically disordered region of FBP21 binds to an extended surface of the C-terminal Sec63 unit of Brr2. Additional contacts in the C-terminal helicase cassette are required for allosteric inhibition of Brr2 helicase activity. Furthermore, the direct interaction between FBP21 and the U4/U6 di-snRNA was found to reduce the pool of unwound U4/U6 di-snRNA. Our results suggest FBP21 as a novel key player in the regulation of Brr2.