Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling

Fu-Lung Yeh, Shang-Lin Chang, Golam Rizvee Ahmed, Hsin-I Liu, Luh Tung, Chung-Shu Yeh, Leah Stands Lanier, Corina Maeder, Che-Min Lin, Shu-Chun Tsai, Wan-Yi Hsiao, Wei-Hau Chang and Tien-Hsien Chang ()
Additional contact information
Fu-Lung Yeh: Academia Sinica
Shang-Lin Chang: Academia Sinica
Golam Rizvee Ahmed: Academia Sinica
Hsin-I Liu: Academia Sinica
Luh Tung: Academia Sinica
Chung-Shu Yeh: Academia Sinica
Leah Stands Lanier: Washington and Lee University
Corina Maeder: Trinity University
Che-Min Lin: Academia Sinica
Shu-Chun Tsai: Academia Sinica
Wan-Yi Hsiao: Academia Sinica
Wei-Hau Chang: Academia Sinica
Tien-Hsien Chang: Academia Sinica

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: Abstract Splicing, a key step in the eukaryotic gene-expression pathway, converts precursor messenger RNA (pre-mRNA) into mRNA by excising introns and ligating exons. This task is accomplished by the spliceosome, a macromolecular machine that must undergo sequential conformational changes to establish its active site. Each of these major changes requires a dedicated DExD/H-box ATPase, but how these enzymes are activated remain obscure. Here we show that Prp28, a yeast DEAD-box ATPase, transiently interacts with the conserved 5′ splice-site (5′SS) GU dinucleotide and makes splicing-dependent contacts with the U1 snRNP protein U1C, and U4/U6.U5 tri-snRNP proteins, Prp8, Brr2, and Snu114. We further show that Prp28’s ATPase activity is potentiated by the phosphorylated Npl3, but not the unphosphorylated Npl3, thus suggesting a strategy for regulating DExD/H-box ATPases. We propose that Npl3 is a functional counterpart of the metazoan-specific Prp28 N-terminal region, which can be phosphorylated and serves as an anchor to human spliceosome.

Date: 2021
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-021-23459-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23459-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-23459-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().