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News and Views
Nature Structural & Molecular Biology 13, 472 - 474 (2006)
doi:10.1038/nsmb0606-472

Splicing fidelity revisited

Charles C Query1 & Maria M Konarska2

1  Charles C Query is in the Dept. of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA. query@aecom.yu.edu

2  Maria M. Konarska is at The Rockefeller University, New York, New York 10021, USA. konarsk@mail.rockefeller.edu

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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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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