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FEBS Lett. 2010 Nov 5;584(21):4408-12. doi: 10.1016/j.febslet.2010.09.043. Epub 2010 Oct 1.

A disulfide linkage in a CCCH zinc finger motif of an Arabidopsis CPSF30 ortholog.

Author information

1
Department of Chemistry, University of Cincinnati, Cincinnati, OH 45221-0172, USA. balasual@ucmail.uc.edu

Abstract

The Arabidopsis ortholog of the 30kDa subunit of the cleavage and polyadenylation factor (AtCPSF30) is an RNA binding endonuclease, and the endonuclease activity is inhibited by reducing agents. Here, we report the presence of a disulfide linkage in the endonuclease motif based on comparative mass spectrometry (MS) analysis of reduced and non-reduced but carbamidomethylated protein. This analysis reveals that this disulfide bond involves a CCCH zinc finger motif, one that is associated with the endonuclease activity of AtCPSF30. This finding raises the possibility that redox regulation of AtCPSF30 may occur through oxidation and reduction of the disulfide linkage.

PMID:
20888817
DOI:
10.1016/j.febslet.2010.09.043
[Indexed for MEDLINE]
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