This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 139/2/857    most recent pp.105.065680v1 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 ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via ISI Web of Science (3) Citing Articles via Google Scholar Google Scholar Articles by Havecker, E. R. Articles by Voytas, D. F. Search for Related Content PubMed PubMed Citation Articles by Havecker, E. R. Articles by Voytas, D. F. Agricola Articles by Havecker, E. R. Articles by Voytas, D. F.

GENETICS, GENOMICS, AND MOLECULAR EVOLUTION

The Sireviruses, a Plant-Specific Lineage of the Ty1/copia Retrotransposons, Interact with a Family of Proteins Related to Dynein Light Chain 8^[w]

Department of Genetics, Development and Cell Biology, Iowa State University, Ames, Iowa 50011

Plant genomes are rich in long terminal repeat retrotransposons, and here we describe a plant-specific lineage of Ty1/copia elements called the Sireviruses. The Sireviruses vary greatly in their genomic organization, and many have acquired additional coding information in the form of an envelope-like open reading frame and an extended gag gene. Two-hybrid screens were conducted with the novel domain of Gag (the Gag extension) encoded by a representative Sirevirus from maize (Zea mays) called Hopie. The Hopie Gag extension interacts with a protein related to dynein light chain 8 (LC8). LC8 also interacts with the Gag extension from a Hopie homolog from rice (Oryza sativa). Amino acid motifs were identified in both Hopie Gag and LC8 that are responsible for the interaction. Two amino acids critical for Gag recognition map within the predicted LC8-binding cleft. Two-hybrid screens were also conducted with the Gag extension encoded by the soybean (Glycine max) SIRE1 element, and an interaction was found with light chain 6 (LC6), a member of the LC8 protein family. LC8 and LC6 proteins are components of the dynein microtubule motor, with LC8 being a versatile adapter that can bind many unrelated cellular proteins and viruses. Plant LC8 and LC6 genes are abundant and divergent, yet flowering plants do not encode other components of the dynein motor. Although, to our knowledge, no cellular roles for plant LC8 family members have been proposed, we hypothesize that binding of LC8 proteins to Gag aids in the movement of retrotransposon virus-like particles within the plant cell or possibly induces important conformational changes in the Gag protein.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.065680.

^* Corresponding author; e-mail voytas{at}iastate.edu; fax 515–294–7155.

Received May 14, 2005; returned for revision July 17, 2005; accepted July 19, 2005.

This article has been cited by other articles:

				C. A. Tanner, P. Rompolas, R. S. Patel-King, O. Gorbatyuk, K.-i. Wakabayashi, G. J. Pazour, and S. M. King Three Members of the LC8/DYNLL Family Are Required for Outer Arm Dynein Motor Function Mol. Biol. Cell, September 1, 2008; 19(9): 3724 - 3734. [Abstract] [Full Text] [PDF]

				X. Gao, Y. Hou, H. Ebina, H. L. Levin, and D. F. Voytas Chromodomains direct integration of retrotransposons to heterochromatin Genome Res., March 1, 2008; 18(3): 359 - 369. [Abstract] [Full Text] [PDF]

				D. Holligan, X. Zhang, N. Jiang, E. J. Pritham, and S. R. Wessler The Transposable Element Landscape of the Model Legume Lotus japonicus Genetics, December 1, 2006; 174(4): 2215 - 2228. [Abstract] [Full Text] [PDF]