» Articles » PMID: 29390077

Cwc23 is a Component of the NTR Complex and Functions to Stabilize Ntr1 and Facilitate Disassembly of Spliceosome Intermediates

Overview
Specialty Biochemistry
Date 2018 Feb 2
PMID 29390077
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

Cwc23 is a member of the J protein family, and has been shown to interact with Ntr1, a scaffold protein that interacts with Ntr2 and Prp43 to form the NTR complex that mediates spliceosome disassembly. We show that Cwc23 is also an intrinsic component of the NTR complex, and that it interacts with the carboxyl terminus of Ntr1. Metabolic depletion of Cwc23 concurrently depleted Ntr1 and Ntr2, suggesting a role for Cwc23 in stabilizing these two proteins. Ntr1, Ntr2 and Cwc23 are stoichiometrically balanced, and form a stable heterotrimer. Depletion of Cwc23 from splicing extracts using antibodies resulted in depletion of all three proteins and accumulation of intron-lariat in the splicing reaction. Cwc23 is not required for disassembly of intron-lariat spliceosome (ILS), but facilitates disassembly of spliceosome intermediates after the actions of Prp2 and Prp16 by stabilizing the association of Ntr1 with the spliceosome. Cwc23 has a more limited effect on the association of Ntr1 with the ILS. Our data suggest that Cwc23 is important for maintaining the levels of Ntr1 and Ntr2, and that it also plays a regulatory role in targeting spliceosome intermediates for disassembly.

Citing Articles

Intron lariat spliceosomes convert lariats to true circles: implications for intron transposition.

Ares Jr M, Igel H, Katzman S, Donohue J Genes Dev. 2024; 38(7-8):322-335.

PMID: 38724209 PMC: 11146597. DOI: 10.1101/gad.351764.124.


Intron-lariat spliceosomes convert lariats to true circles: implications for intron transposition.

Ares Jr M, Igel H, Katzman S, Donohue J bioRxiv. 2024; .

PMID: 38585890 PMC: 10996645. DOI: 10.1101/2024.03.26.586863.


Arresting Spliceosome Intermediates at Various Stages of the Splicing Pathway.

Tseng C, Cheng S Methods Mol Biol. 2023; 2666:193-211.

PMID: 37166667 DOI: 10.1007/978-1-0716-3191-1_15.


Mechanisms of germ cell survival and plasticity in Caenorhabditis elegans.

Cao W, Pocock R Biochem Soc Trans. 2022; 50(5):1517-1526.

PMID: 36196981 PMC: 9704514. DOI: 10.1042/BST20220878.


Termination of pre-mRNA splicing requires that the ATPase and RNA unwindase Prp43p acts on the catalytic snRNA U6.

Toroney R, Nielsen K, Staley J Genes Dev. 2019; 33(21-22):1555-1574.

PMID: 31558568 PMC: 6824469. DOI: 10.1101/gad.328294.119.


References
1.
Lebaron S, Papin C, Capeyrou R, Chen Y, Froment C, Monsarrat B . The ATPase and helicase activities of Prp43p are stimulated by the G-patch protein Pfa1p during yeast ribosome biogenesis. EMBO J. 2009; 28(24):3808-19. PMC: 2797057. DOI: 10.1038/emboj.2009.335. View

2.
Zhang L, Xu T, Maeder C, Bud L, Shanks J, Nix J . Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2. Nat Struct Mol Biol. 2009; 16(7):731-9. PMC: 2743687. DOI: 10.1038/nsmb.1625. View

3.
Tseng C, Liu H, Cheng S . DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps. RNA. 2010; 17(1):145-54. PMC: 3004056. DOI: 10.1261/rna.2459611. View

4.
Liu H, Cheng S . The interaction of Prp2 with a defined region of the intron is required for the first splicing reaction. Mol Cell Biol. 2012; 32(24):5056-66. PMC: 3510548. DOI: 10.1128/MCB.01109-12. View

5.
Tarn W, Hsu C, Huang K, Chen H, Kao H, Lee K . Functional association of essential splicing factor(s) with PRP19 in a protein complex. EMBO J. 1994; 13(10):2421-31. PMC: 395108. DOI: 10.1002/j.1460-2075.1994.tb06527.x. View