- THIS ARTICLE
- Full Text
- Full Text (PDF)
-
All Versions of this Article:
genetics.106.063826v1
176/1/409 most recent - Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Email this article to a friend
- 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 Carré-Mlouka, A.
- Articles by Contamine, D.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Carré-Mlouka, A.
- Articles by Contamine, D.
Originally published as Genetics Published Articles Ahead of Print on April 3, 2007.
Genetics, Vol. 176, 409-419, May 2007, Copyright © 2007
doi:10.1534/genetics.106.063826
Control of Sigma Virus Multiplication by the ref(2)P Gene of Drosophila melanogaster: An in Vivo Study of the PB1 Domain of Ref(2)P
A. Carré-Mlouka*,1,
S. Gaumer*,1,
P. Gay*,
A. M. Petitjean*,
C. Coulondre*,
P. Dru
,
F. Bras
,
S. Dezélée and
D. Contamine*,2
* Université Versailles SQY, CNRS, Laboratoire de Génétique et Biologie Cellulaire–UMR 8159, 78035 Versailles, France, BioMarCell–UMR 7009, CNRS/Université Paris VI, Station Zoologique, Observatoire, 06230 Villefranche/Mer, France and UMR de Virologie Moléculaire et Structurale, CNRS 2472–INRA 1157, 91198 Gif/Yvette, France
2 Corresponding author: Université Versailles-St. Quentin-en-Yvelines, LGBC, 45 av. des Etats-Unis, 78035 Versailles Cedex, France.
E-mail: didier.contamine{at}uvsq.fr
Ref(2)P has been described as one of the Drosophila proteins that interacts with the sigma virus cycle. We generated alleles to identify critical residues involved in the restrictive (inhibiting viral multiplication) or permissive (allowing viral multiplication) character of Ref(2)P. We demonstrate that permissive alleles increase the ability of the sigma virus to infect Drosophila when compared to null alleles and we confirm that restrictive alleles decrease this capacity. Moreover, we have created alleles unfunctional in viral cycling while functional for Ref(2)P fly functions. This type of allele had never been observed before and shows that fly- and virus-related activities of Ref(2)P are separable. The viral status of Ref(2)P variants is determined by the amino-terminal PB1 domain polymorphism. In addition, an isolated PB1 domain mimics virus-related functions even if it is similar to a loss of function toward fly-related activities. The evolutionary tree of the Ref(2)P PB1 domain that we could build on the basis of the natural allele sequences is in agreement with an evolution of PB1 domain due to successive transient selection waves.
This article has been cited by other articles:
 |
|
 |
|
  J. Bangham, K.-W. Kim, C. L. Webster, and F. M. Jiggins Genetic Variation Affecting Host-Parasite Interactions: Different Genes Affect Different Aspects of Sigma Virus Replication and Transmission in Drosophila melanogaster Genetics, April 1, 2008; 178(4): 2191 - 2199. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. P. Nezis, A. Simonsen, A. P. Sagona, K. Finley, S. Gaumer, D. Contamine, T. E. Rusten, H. Stenmark, and A. Brech Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain J. Cell Biol., March 24, 2008; 180(6): 1065 - 1071. [Abstract] [Full Text] [PDF]
|
|