- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Simonelig, M.
- Articles by O'Hare, K.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Simonelig, M.
- Articles by O'Hare, K.
Genetics, Vol 142, 1225-1235, Copyright © 1996
INVESTIGATIONS |
Interallelic Complementation at the suppressor of forked Locus of Drosophila Reveals Complementation Between Suppressor of forked Proteins Mutated in Different Regions
M. Simonelig, K. Elliott, A. Mitchelson and K. O'Hare
Dynamique du Genome et Evolution, Institut Jacques Monod, Universite Paris 7, 75005 Paris, France
The Su(f) protein of Drosophila melanogaster shares extensive homologies with proteins from yeast (RNA14) and man (77 kD subunit of cleavage stimulation factor) that are required for 3' end processing of mRNA. These homologies suggest that su(f) is involved in mRNA 3' end formation and that some aspects of this process are conserved throughout eukaryotes. We have investigated the genetic and molecular complexity of the su(f) locus. The su(f) gene is transcribed to produce three RNAs and could encode two proteins. Using constructs that contain different parts of the locus, we show that only the larger predicted gene product of 84 kD is required for the wild-type function of su(f). Some lethal alleles of su(f) complement to produce viable combinations. The structures of complementing and noncomplementing su(f) alleles indicate that 84-kD Su(f) proteins mutated in different domains can act in combination for partial su(f) function. Our results suggest protein-protein interaction between or within wild-type Su(f) molecules.
This article has been cited by other articles:
![]() |
P. Legrand, N. Pinaud, L. Minvielle-Sebastia, and S. Fribourg The structure of the CstF-77 homodimer provides insights into CstF assembly Nucleic Acids Res., July 26, 2007; 35(13): 4515 - 4522. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. Benoit, F. Juge, F. Iral, A. Audibert, and M. Simonelig Chimeric human CstF-77/Drosophila Suppressor of forked proteins rescue suppressor of forked mutant lethality and mRNA 3' end processing in Drosophila PNAS, August 6, 2002; 99(16): 10593 - 10598. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Takagaki and J. L. Manley Complex Protein Interactions within the Human Polyadenylation Machinery Identify a Novel Component Mol. Cell. Biol., March 1, 2000; 20(5): 1515 - 1525. [Abstract] [Full Text] |
||||
![]() |
B. Benoit, A. Nemeth, N. Aulner, U. Kuhn, M. Simonelig, E. Wahle, and H. M. Bourbon The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitro Nucleic Acids Res., October 1, 1999; 27(19): 3771 - 3778. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Audibert and M. Simonelig Autoregulation at the level of mRNA 3' end formation of the suppressor of forked gene of Drosophila melanogaster is conserved in Drosophila virilis PNAS, November 24, 1998; 95(24): 14302 - 14307. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. F. Colgan and J. L. Manley Mechanism and regulation of mRNA polyadenylation Genes & Dev., November 1, 1997; 11(21): 2755 - 2766. [Full Text] [PDF] |
||||



