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The Dominant Temperature-Sensitive Lethal DTS7 of Drosophila melanogaster Encodes an Altered 20S Proteasome ß-Type Subunit
Kerrie A. Smytha and John M. Beloteaa Department of Biology, Syracuse University, Syracuse, New York 13244
Corresponding author: John M. Belote, Department of Biology, Syracuse University, 130 College Place, Syracuse, NY 13244., jbelote{at}mailbox.syr.edu (E-mail)
Communicating editor: L. L. SEARLES
-type and 7 ß-type. DTS7 is a dominant temperature-sensitive (DTS) lethal mutation at 29° that also acts as a recessive lethal at ambient temperatures. DTS7 maps to cytological position 71AB. Molecular characterization of DTS7 reveals that this is caused by a missense mutation in a ß-type subunit gene, ß2. A previously characterized DTS mutant, l(3)73Ai1, results from a missense mutation in another ß-type subunit gene, ß6. These two mutants share a very similar phenotype, show a strong allele-specific genetic interaction, and are rescued by the same extragenic suppressor, Su(DTS)-1. We propose that these mutants might act as "poison subunits," disrupting proteasome function in a dosage-dependent manner, and suggest how they may interact on the basis of the structure of the yeast 20S proteasome.
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