|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print November 10, 2005
Plant and Soil Sciences, University of Kentucky, Lexington, KY 40546-0312
Corresponding Author: aghunt00{at}uky.edu
The protein Fip1 is an important subunit of the eukaryotic polyadenylation apparatus, as it provides a bridge of sorts between poly(A) polymerase, other subunits of the polyadenylation apparatus, and the substrate RNA. In this study, a previously-unreported Arabidopsis Fip1 homolog is characterized. The gene for this protein resides on chromosome V and encodes an 1196 amino acid polypeptide. Yeast two-hybrid and in vitro assays indicate that the N-terminal 137 amino acids of the Arabidopsis Fip1 protein interact with poly(A) polymerase (PAP). This domain also stimulates the activity of the PAP. Interestingly, this part of the Arabidopsis Fip1 interacts with Arabidopsis homologs of CstF77, CPSF30, CFIm-25, and PabN1. The interactions with CstF77, CPSF30, and CFIm-25 are reminiscent in various respects of similar interactions seen in yeast and mammals, even though the part of the Arabidopsis Fip1 protein that participates in these interactions has no apparent counterpart in other eukaryotic Fip1 proteins. Interactions between Fip1 and PabN1 have not been reported in other systems; this may represent plant-specific associations. The C-terminal 789 amino acids of the Arabidopsis Fip1 protein were found to contain an RNA-binding domain; this domain correlated with an intact arginine-rich region and had a marked preference for poly(G) among the four homopolymers studied. These results indicate that the Arabidopsis Fip1, like its human counterpart, is an RNA-binding protein. Moreover, they provide conceptual links between PAP and several other Arabidopsis polyadenylation factor subunit homologs.
J. Biol. Chem, 10.1074/jbc.M510964200
Submitted on October 7, 2005
Revised on November 2, 2005
Accepted on November 10, 2005
An Arabidopsis Fip1 homologue interacts with RNA and provides conceptual links with a number of other polyadenylation factor subunits
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  D. Xing, H. Zhao, and Q. Q. Li Arabidopsis CLP1-SIMILAR PROTEIN3, an Ortholog of Human Polyadenylation Factor CLP1, Functions in Gametophyte, Embryo, and Postembryonic Development Plant Physiology, December 1, 2008; 148(4): 2059 - 2069. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Addepalli and A. G. Hunt A novel endonuclease activity associated with the Arabidopsis ortholog of the 30-kDa subunit of cleavage and polyadenylation specificity factor Nucleic Acids Res., July 26, 2007; 35(13): 4453 - 4463. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. J. Herr, A. Molnar, A. Jones, and D. C. Baulcombe Inaugural Article: Defective RNA processing enhances RNA silencing and influences flowering of Arabidopsis PNAS, October 10, 2006; 103(41): 14994 - 15001. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. J. Delaney, R. Xu, J. Zhang, Q. Q. Li, K.-Y. Yun, D. L. Falcone, and A. G. Hunt Calmodulin Interacts with and Regulates the RNA-Binding Activity of an Arabidopsis Polyadenylation Factor Subunit Plant Physiology, April 1, 2006; 140(4): 1507 - 1521. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |