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

Balasubrahmanyam Addepalli, Patrick A. Limbach, Arthur G. Hunt

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


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.

Original languageEnglish
Pages (from-to)4408-4412
Number of pages5
JournalFEBS Letters
Issue number21
StatePublished - Nov 5 2010

Bibliographical note

Funding Information:
The authors are grateful to Drs. Stephen F Macha and Larry Sallans for technical guidance in conducting mass spectrometry analysis. This work was supported by National Science Foundation Grants MCB -0313472 and IOS-0817818 (to A.G.H.) and CHE 0602413 and CHE 0910751 (to P.A.L.). Appendix A


  • CCCH zinc finger
  • CPSF30
  • Disulfide linkage
  • Endonuclease
  • Mass spectrometry

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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