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Molecular and Cellular Biology, October 2001, p. 6808-6819, Vol. 21, No. 20
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.20.6808-6819.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Developmental and Transcriptional Consequences of Mutations in Drosophila TAF_II60

Norikazu Aoyagi and David A. Wassarman^*

Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892

Received 7 June 2001/Returned for modification 2 July 2001/Accepted 12 July 2001

In vitro, the TAF_II60 component of the TFIID complex contributes to RNA polymerase II transcription initiation by serving as a coactivator that interacts with specific activator proteins and possibly as a promoter selectivity factor that interacts with the downstream promoter element. In vivo roles for TAF_II60 in metazoan transcription are not as clear. Here we have investigated the developmental and transcriptional requirements for TAF_II60 by analyzing four independent Drosophila melanogaster TAF_II60 mutants. Loss-of-function mutations in Drosophila TAF_II60 result in lethality, indicating that TAF_II60 provides a nonredundant function in vivo. Molecular analysis of TAF_II60 alleles revealed that essential TAF_II60 functions are provided by two evolutionarily conserved regions located in the N-terminal half of the protein. TAF_II60 is required at all stages of Drosophila development, in both germ cells and somatic cells. Expression of TAF_II60 from a transgene rescued the lethality of TAF_II60 mutants and exposed requirements for TAF_II60 during imaginal development, spermatogenesis, and oogenesis. Phenotypes of rescued TAF_II60 mutant flies implicate TAF_II60 in transcriptional mechanisms that regulate cell growth and cell fate specification and suggest that TAF_II60 is a limiting component of the machinery that regulates the transcription of dosage-sensitive genes. Finally, TAF_II60 plays roles in developmental regulation of gene expression that are distinct from those of other TAF_II proteins.

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^* Corresponding author. Present address: Department of Pharmacology, University of Wisconsin Medical School, 1300 University Ave., Madison, WI 53706. Phone: (608) 262-6648. Fax: (608) 262-1257. E-mail: dawassarman{at}facstaff.wisc.edu.

Present address: Department of Biological Science and Technology, Science University of Tokyo, Noda, Chiba 278-8510, Japan.

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Molecular and Cellular Biology, October 2001, p. 6808-6819, Vol. 21, No. 20
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.20.6808-6819.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

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