Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (8)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Yao, Y.
Right arrow Articles by Galili, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yao, Y.
Right arrow Articles by Galili, G.
Agricola
Right arrow Articles by Yao, Y.
Right arrow Articles by Galili, G.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

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

Youli Yao, Luhua Song, Yael Katz and Gad Galili1,

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.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Plant Cell PhysiolHome page
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]


Home page
Proc. Natl. Acad. Sci. USAHome page
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]


Home page
J. Biol. Chem.Home page
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]


Home page
J. Biol. Chem.Home page
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]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.