Journal of Experimental Botany, Vol. 53, No. 378, pp. 2277-2278,
November 1, 2002
© 2002 Oxford University Press
Cloning and characterization of Arabidopsis homologues of the animal CstF complex that regulates 3' mRNA cleavage and polyadenylation
Received 11 June 2002; Accepted 3 July 2002
Department of Plant Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel
1 To whom correspondence should be addressed. Fax: +972 8 9344181. E-mail: gad.galili{at}weizmann.ac.il
The 3' cleavage and polyadenylation of mRNAs has been studied in detail in animals and yeast, but not in plants. Aimed at elucidating the regulation of mRNA 3' end formation in plants, three Arabidopsis cDNAs encoding homologues of the animal proteins CstF-64, CstF-77 and CstF-50 that form the cleavage stimulating factor of the polyadenylation machinery have been cloned. It is shown experimentally that the N-terminal domain of the Arabidopsis CstF-64 homologue binds the mRNA 3' non-coding region in an analogous manner to the animal protein. It is also shown that the Arabidopsis CstF-64 and CstF-77 homologues strongly interact with each other in a similar way to their animal counterparts. These results imply that these Arabidopsis homologues belong to the polyadenylation machinery of nuclear mRNAs.
Key words: Key words: Arabidopsis, CstF complex, mRNA cleavage and polyadenylation, regulation.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
Y. H. Jang, H.-Y. Park, S.-K. Kim, J. H. Lee, M. C. Suh, Y. S. Chung, K.-H. Paek, and J.-K. Kim Survey of Rice Proteins Interacting With OsFCA and OsFY Proteins Which Are Homologous to the Arabidopsis Flowering Time Proteins, FCA and FY Plant Cell Physiol., August 1, 2009; 50(8): 1479 - 1492. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Manzano, S. Marquardt, A. M. E. Jones, I. Baurle, F. Liu, and C. Dean Altered interactions within FY/AtCPSF complexes required for Arabidopsis FCA-mediated chromatin silencing PNAS, May 26, 2009; 106(21): 8772 - 8777. [Abstract] [Full Text] [PDF] |
||||
![]() |
X. Qu, J.-M. Perez-Canadillas, S. Agrawal, J. De Baecke, H. Cheng, G. Varani, and C. Moore The C-terminal Domains of Vertebrate CstF-64 and Its Yeast Orthologue Rna15 Form a New Structure Critical for mRNA 3'-End Processing J. Biol. Chem., January 19, 2007; 282(3): 2101 - 2115. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. P. Forbes, B. Addepalli, and A. G. Hunt An Arabidopsis Fip1 Homolog Interacts with RNA and Provides Conceptual Links with a Number of Other Polyadenylation Factor Subunits J. Biol. Chem., January 6, 2006; 281(1): 176 - 186. [Abstract] [Full Text] [PDF] |
||||


