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

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

doi:10.1016/j.febslet.2010.09.043

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 journal › Article › peer-review

17 Scopus citations

Abstract

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 language	English
Pages (from-to)	4408-4412
Number of pages	5
Journal	FEBS Letters
Volume	584
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2010.09.043
State	Published - 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

Keywords

CCCH zinc finger
CPSF30
Disulfide linkage
Endonuclease
Mass spectrometry

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/j.febslet.2010.09.043

Cite this

@article{d88f234bcc13474784e88d24b166f905,

title = "A disulfide linkage in a CCCH zinc finger motif of an Arabidopsis CPSF30 ortholog",

abstract = "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.",

keywords = "CCCH zinc finger, CPSF30, Disulfide linkage, Endonuclease, Mass spectrometry",

author = "Balasubrahmanyam Addepalli and Limbach, {Patrick A.} and Hunt, {Arthur G.}",

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 ",

year = "2010",

month = nov,

day = "5",

doi = "10.1016/j.febslet.2010.09.043",

language = "English",

volume = "584",

pages = "4408--4412",

number = "21",

}

TY - JOUR

T1 - A disulfide linkage in a CCCH zinc finger motif of an Arabidopsis CPSF30 ortholog

AU - Addepalli, Balasubrahmanyam

AU - Limbach, Patrick A.

AU - Hunt, Arthur G.

N1 - 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

PY - 2010/11/5

Y1 - 2010/11/5

N2 - 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.

AB - 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.

KW - CCCH zinc finger

KW - CPSF30

KW - Disulfide linkage

KW - Endonuclease

KW - Mass spectrometry

UR - http://www.scopus.com/inward/record.url?scp=78049319919&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78049319919&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2010.09.043

DO - 10.1016/j.febslet.2010.09.043

M3 - Article

C2 - 20888817

AN - SCOPUS:78049319919

SN - 0014-5793

VL - 584

SP - 4408

EP - 4412

JO - FEBS Letters

JF - FEBS Letters

IS - 21

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this