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Retrotransposon Target Site Selection by Imitation of a Cellular Protein

Retrotransposon Target Site Selection by Imitation of a Cellular Protein Retrotransposon Target Site Selection by Imitation of a Cellular Protein ▿ † Troy L. Brady ‡ , Peter G. Fuerst § , Robert A. Dick , Clarice Schmidt and Daniel F. Voytas * Department of Genetics, Development, and Cell Biology, 1035A Roy J. Carver Co-Laboratory, Iowa State University, Ames, Iowa 50011 ABSTRACT Mobile elements rely on cellular processes to replicate, and therefore, mobile element proteins frequently interact with a variety of cellular factors. The integrase (IN) encoded by the retrotransposon Ty5 interacts with the heterochromatin protein Sir4, and this interaction determines Ty5's preference to integrate into heterochromatin. We explored the hypothesis that Ty5's targeting mechanism arose by mimicking an interaction between Sir4 and another cellular protein(s). Mutational analyses defined the requirements for the IN-Sir4 interaction, providing criteria to screen for cellular analogues. Esc1, a protein associated with the inner nuclear membrane, interacted with the same domain of Sir4 as IN, and 75% of mutations that disrupted IN-Sir4 interactions also abrogated Esc1-Sir4 interactions. A small motif critical for recognizing Sir4 was identified in Esc1. The functional equivalency of this motif and the Sir4-interacting domain of IN was demonstrated by swapping these motifs and showing that the chimeric IN and Esc1 proteins effectively target integration and partition DNA, respectively. We conclude that Ty5 targets integration by imitating the Esc1-Sir4 interaction and suggest molecular mimicry as a general mechanism that enables mobile elements to interface with cellular processes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular and Cellular Biology American Society For Microbiology

Retrotransposon Target Site Selection by Imitation of a Cellular Protein

Retrotransposon Target Site Selection by Imitation of a Cellular Protein

Molecular and Cellular Biology , Volume 28 (4): 1230 – Feb 15, 2008

Abstract

Retrotransposon Target Site Selection by Imitation of a Cellular Protein ▿ † Troy L. Brady ‡ , Peter G. Fuerst § , Robert A. Dick , Clarice Schmidt and Daniel F. Voytas * Department of Genetics, Development, and Cell Biology, 1035A Roy J. Carver Co-Laboratory, Iowa State University, Ames, Iowa 50011 ABSTRACT Mobile elements rely on cellular processes to replicate, and therefore, mobile element proteins frequently interact with a variety of cellular factors. The integrase (IN) encoded by the retrotransposon Ty5 interacts with the heterochromatin protein Sir4, and this interaction determines Ty5's preference to integrate into heterochromatin. We explored the hypothesis that Ty5's targeting mechanism arose by mimicking an interaction between Sir4 and another cellular protein(s). Mutational analyses defined the requirements for the IN-Sir4 interaction, providing criteria to screen for cellular analogues. Esc1, a protein associated with the inner nuclear membrane, interacted with the same domain of Sir4 as IN, and 75% of mutations that disrupted IN-Sir4 interactions also abrogated Esc1-Sir4 interactions. A small motif critical for recognizing Sir4 was identified in Esc1. The functional equivalency of this motif and the Sir4-interacting domain of IN was demonstrated by swapping these motifs and showing that the chimeric IN and Esc1 proteins effectively target integration and partition DNA, respectively. We conclude that Ty5 targets integration by imitating the Esc1-Sir4 interaction and suggest molecular mimicry as a general mechanism that enables mobile elements to interface with cellular processes.

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References (61)

Publisher
American Society For Microbiology
Copyright
Copyright © 2008 by the American society for Microbiology.
ISSN
0270-7306
eISSN
1098-5549
DOI
10.1128/MCB.01502-07
pmid
18086891
Publisher site
See Article on Publisher Site

Abstract

Retrotransposon Target Site Selection by Imitation of a Cellular Protein ▿ † Troy L. Brady ‡ , Peter G. Fuerst § , Robert A. Dick , Clarice Schmidt and Daniel F. Voytas * Department of Genetics, Development, and Cell Biology, 1035A Roy J. Carver Co-Laboratory, Iowa State University, Ames, Iowa 50011 ABSTRACT Mobile elements rely on cellular processes to replicate, and therefore, mobile element proteins frequently interact with a variety of cellular factors. The integrase (IN) encoded by the retrotransposon Ty5 interacts with the heterochromatin protein Sir4, and this interaction determines Ty5's preference to integrate into heterochromatin. We explored the hypothesis that Ty5's targeting mechanism arose by mimicking an interaction between Sir4 and another cellular protein(s). Mutational analyses defined the requirements for the IN-Sir4 interaction, providing criteria to screen for cellular analogues. Esc1, a protein associated with the inner nuclear membrane, interacted with the same domain of Sir4 as IN, and 75% of mutations that disrupted IN-Sir4 interactions also abrogated Esc1-Sir4 interactions. A small motif critical for recognizing Sir4 was identified in Esc1. The functional equivalency of this motif and the Sir4-interacting domain of IN was demonstrated by swapping these motifs and showing that the chimeric IN and Esc1 proteins effectively target integration and partition DNA, respectively. We conclude that Ty5 targets integration by imitating the Esc1-Sir4 interaction and suggest molecular mimicry as a general mechanism that enables mobile elements to interface with cellular processes.

Journal

Molecular and Cellular BiologyAmerican Society For Microbiology

Published: Feb 15, 2008

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