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

The Arabidopsis ortholog of the 30 kDa 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...

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Veröffentlicht in:	FEBS letters 2010-11, Vol.584 (21), p.4408-4412
Hauptverfasser:	Addepalli, Balasubrahmanyam, Limbach, Patrick A., Hunt, Arthur G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Arabidopsis Arabidopsis Proteins - chemistry Arabidopsis Proteins - metabolism Biocatalysis CCCH zinc finger Chromatography, Liquid Cleavage And Polyadenylation Specificity Factor - chemistry Cleavage And Polyadenylation Specificity Factor - metabolism CPSF30 Disulfide linkage Disulfides - chemistry Endonuclease Endonucleases - metabolism Mass spectrometry Molecular Sequence Data Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Tandem Mass Spectrometry Zinc Fingers
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Zusammenfassung:	The Arabidopsis ortholog of the 30 kDa 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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2010.09.043