FEBS Letters
Volume 584, Issue 8 , Pages 1449-1454, 16 April 2010

The Arabidopsis ortholog of the 77kDa subunit of the cleavage stimulatory factor (AtCstF-77) involved in mRNA polyadenylation is an RNA-binding protein

Edited by Tamas Dalmay

University of Kentucky, Department of Plant and Soil Sciences, Plant Physiology Program, 1405 Veterans Drive, 345 Plant Science Building, Lexington, KY 40506-0312, USA

Received 15 January 2010; received in revised form 23 February 2010; accepted 3 March 2010. published online 08 March 2010.

Abstract 

The 77kDa subunit of the polyadenylation cleavage stimulation factor (CstF77) is important in messenger RNA 3′ end processing. Previously, we demonstrated that AtCstF77 interacts with AtCPSF30, the Arabidopsis ortholog of the 30kDa subunit of the Cleavage and Polyadenylation Specificity Factor. In further dissecting this interaction, it was found that the C-terminus of AtCstF77 interacts with AtCPSF30. Remarkably, we also found that the C-terminal domain of AtCstF77 possesses RNA-binding ability. These studies therefore reveal AtCstF77 to be an RNA-binding protein, adding yet another RNA-binding activity to the plant polyadenylation complex. This raises interesting questions as to the means by which RNAs are recognized during mRNA 3′ end formation in plants.

Structured summary:

MINT-7712550: AtCstF77 (uniprotkb:Q8LKG5) binds (MI:0407) to AtCPSF30 (uniprotkb:A9LNK9) by pull down (MI:0096)

Keywords: Polyadenylation, CstF77, CPSF30, RNA-binding

Abbreviations: CstF, cleavage stimulatory factor, CPSF, cleavage and polyadenylation specificity factor, RRM, RNA recognition motif, MBP, maltose binding protein

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(10)00201-2

doi:10.1016/j.febslet.2010.03.007

FEBS Letters
Volume 584, Issue 8 , Pages 1449-1454, 16 April 2010