An in vivo analysis of the vestigial gene in Drosophila melanogaster defines the domains required for Vg function.
Considerable evidence indicates an obligate partnership of the Drosophila melanogaster Vestigial (VG) and Scalloped (SD) proteins within the context of wing development. These two proteins interact physically and a 56-amino-acid motif within VG is necessary and sufficient for this binding. While the importance of this SD-binding domain has been clearly demonstrated both in vitro and in vivo, the remaining portions of VG have not been examined for in vivo function. Herein, additional regions within VG were tested for possible in vivo functions. The results identify two additional domains that must be present for optimal VG function as measured by the loss of ability to rescue vg mutants, to induce ectopic sd expression, and to perform other normal VG functions when they are deleted. An in vivo study such as this one is fundamentally important because it identifies domains of VG that are necessary in the cellular context in which wing development actually occurs. The results also indicate that an additional large portion of VG, outside of these two domains and the SD-binding domain, is dispensable in the execution of these normal VG functions.
MacKay
Julie O
JO
Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2E9, Canada.
Soanes
Kelly H
KH
Srivastava
Ajay
A
Simmonds
Andrew
A
Brook
William J
WJ
Bell
John B
JB
D000818:Animals; D029721:Drosophila Proteins / Q000235:genetics* / Q000378:metabolism; D004331:Drosophila melanogaster / Q000235:genetics* / Q000378:metabolism; D009687:Nuclear Proteins / Q000235:genetics* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D017384:Sequence Deletion; D014921:Wings, Animal / Q000254:growth & development*
D029721:Drosophila Proteins; D009687:Nuclear Proteins; C095064:vg protein, Drosophila