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

Yeast helicase Prp28 promotes the first step of spliceosome remodeling. By placing a photoactivatable unnatural amino acid in Prp28, the authors capture Prp28 in action revealing its dynamic interactions and cofactor Npl3.

Bibliographic Details
Main Authors:	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, Tien-Hsien Chang
Format:	Article
Language:	English
Published:	Nature Publishing Group 2021-05-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-021-23459-4

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spelling	doaj-9e81c7d52d55433ab0c6e27d3c0010652021-05-30T11:14:38ZengNature Publishing GroupNature Communications2041-17232021-05-011211910.1038/s41467-021-23459-4Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodelingFu-Lung Yeh0Shang-Lin Chang1Golam Rizvee Ahmed2Hsin-I Liu3Luh Tung4Chung-Shu Yeh5Leah Stands Lanier6Corina Maeder7Che-Min Lin8Shu-Chun Tsai9Wan-Yi Hsiao10Wei-Hau Chang11Tien-Hsien Chang12Genomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaDepartment of Biology, Washington and Lee UniversityDepartment of Chemistry, Trinity UniversityGenomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaGenomics Research Center, Academia SinicaInstitute of Chemistry, Academia SinicaGenomics Research Center, Academia SinicaYeast helicase Prp28 promotes the first step of spliceosome remodeling. By placing a photoactivatable unnatural amino acid in Prp28, the authors capture Prp28 in action revealing its dynamic interactions and cofactor Npl3.https://doi.org/10.1038/s41467-021-23459-4
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	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 Tien-Hsien Chang
spellingShingle	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 Tien-Hsien Chang Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling Nature Communications
author_facet	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 Tien-Hsien Chang
author_sort	Fu-Lung Yeh
title	Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling
title_short	Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling
title_full	Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling
title_fullStr	Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling
title_full_unstemmed	Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling
title_sort	activation of prp28 atpase by phosphorylated npl3 at a critical step of spliceosome remodeling
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2021-05-01
description	Yeast helicase Prp28 promotes the first step of spliceosome remodeling. By placing a photoactivatable unnatural amino acid in Prp28, the authors capture Prp28 in action revealing its dynamic interactions and cofactor Npl3.
url	https://doi.org/10.1038/s41467-021-23459-4
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Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling

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