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Functional Interaction between the Drosophila Knirps Short Range Transcriptional Repressor and RPD3
 

Summary: Functional Interaction between the Drosophila Knirps
Short Range Transcriptional Repressor and RPD3
Histone Deacetylase*
Received for publication,June 23, 2005, and in revised form, September 26, 2005 Published, JBC Papers in Press,September 26, 2005, DOI 10.1074/jbc.M506819200
Paolo Struffi1
and David N. Arnosti2
From the Department of Biochemistry and Molecular Biology and Program in Genetics, Michigan State University,
East Lansing, Michigan 48824
Knirps and other short range transcriptional repressors play crit-
ical roles in patterning the early Drosophila embryo. These repres-
sors are known to bind the C-terminal binding protein corepressor,
but their mechanism of action is poorly understood. We purified
functional recombinant Knirps protein from transgenic embryos to
identify possible cofactors that contribute to the activity of this pro-
tein. The protein migrates in a complex of 450 kDa and was found
to copurify with the Rpd3 histone deacetylase protein during a dou-
ble affinity purification procedure. Association of Rpd3 with Knirps
was dependent on the presence of the C-terminal binding protein-
dependent repression domain of Knirps. Previous studies of an rpd3
mutant had not shown defects in the pattern of expression of even-

  

Source: Arnosti, David N. - Department of Biochemistry and Molecular Biology, Michigan State University

 

Collections: Biology and Medicine