Splicing fidelity revisited

Charles C. Query; Maria M. Konarska

doi:10.1038/nsmb0606-472

Splicing fidelity revisited

Charles C. Query, Maria M. Konarska

Cell Biology

Research output: Contribution to journal › Short survey › peer-review

24 Scopus citations

Abstract

Since the discovery of Prp16, a spliceosomal ATPase that alters the fidelity of splicing, many other ATPases associated with the spliceosome have been postulated to work similarly. The finding that Prp22, a DEAH-box ATPase, functions as a fidelity factor for the second step of splicing supports this hypothesis.

Original language	English (US)
Pages (from-to)	472-474
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	13
Issue number	6
DOIs	https://doi.org/10.1038/nsmb0606-472
State	Published - Jun 26 2006

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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title = "Splicing fidelity revisited",

abstract = "Since the discovery of Prp16, a spliceosomal ATPase that alters the fidelity of splicing, many other ATPases associated with the spliceosome have been postulated to work similarly. The finding that Prp22, a DEAH-box ATPase, functions as a fidelity factor for the second step of splicing supports this hypothesis.",

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AB - Since the discovery of Prp16, a spliceosomal ATPase that alters the fidelity of splicing, many other ATPases associated with the spliceosome have been postulated to work similarly. The finding that Prp22, a DEAH-box ATPase, functions as a fidelity factor for the second step of splicing supports this hypothesis.

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Splicing fidelity revisited

Abstract

ASJC Scopus subject areas

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