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Articles 1 - 4 of 4
Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
The Spliceosomal Protein Sf3b5 Is A Novel Component Of Drosophila Saga That Functions In Gene Expression Independent Of Splicing, Rachel Stegeman, Peyton J. Spreacker, Selene K. Swanson, Robert Stephenson, Laurence Florens, Michael P. Washburn, Vikki M. Weake
The Spliceosomal Protein Sf3b5 Is A Novel Component Of Drosophila Saga That Functions In Gene Expression Independent Of Splicing, Rachel Stegeman, Peyton J. Spreacker, Selene K. Swanson, Robert Stephenson, Laurence Florens, Michael P. Washburn, Vikki M. Weake
Department of Biochemistry Faculty Publications
The interaction between splicing factors and the transcriptional machinery provides an intriguing link between the coupled processes of transcription and splicing. Here, we show that the two components of the SF3B complex, SF3B3 and SF3B5, that form part of the U2 small nuclear ribonucleoprotein particle (snRNP) are also subunits of the Spt-Ada-Gcn5 acetyltransferase (SAGA) transcriptional coactivator complex in Drosophila melanogaster. Whereas SF3B3 had previously been identified as a human SAGA subunit, SF3B5 had not been identified as a component of SAGA in any species. We show that SF3B3 and SF3B5 bind to SAGA independent of RNA and interact with …
A Screen To Identify Saga-Activated Genes That Are Required For Proper Photoreceptor Axon Targeting In Drosophila Melanogaster, Kaelan J. Brennan, Vikki M. Weake, Jingqun Q. Ma
A Screen To Identify Saga-Activated Genes That Are Required For Proper Photoreceptor Axon Targeting In Drosophila Melanogaster, Kaelan J. Brennan, Vikki M. Weake, Jingqun Q. Ma
The Summer Undergraduate Research Fellowship (SURF) Symposium
The inherited human genetic disease spinocerebellar ataxia type 7 (SCA7) is characterized by progressive neurodegeneration and visual impairment that ultimately leads to blindness. SCA7 results from a mutation in the human ATXN7 gene that causes an expansion of polyglutamine tracts in this gene’s corresponding protein. Human ATXN7 protein serves as a component of the deubiquitylase (DUB) module of the large, multi-subunit complex Spt-Ada-Gcn acetyltransferase, or SAGA. SAGA is a transcriptional coactivator and histone modifier that functions to deubiquitylate histone H2B and allow for transcription of SAGA-mediated genes to occur. In Drosophila, mutations in SAGA DUB’s Nonstop and sgf11 components …
Determining The Binding Between Saga Subunits And Spliceosomal Components, Peyton J. Spreacker, Rachel L. Stegeman, Vikki M. Weake
Determining The Binding Between Saga Subunits And Spliceosomal Components, Peyton J. Spreacker, Rachel L. Stegeman, Vikki M. Weake
The Summer Undergraduate Research Fellowship (SURF) Symposium
Proper gene regulation is vital to the health and development of an organism. Determining the relationship between splicing, transcription, and chromatin structure is vital for understanding gene regulation as a whole. There have been previous studies linking these elements pairwise; however, no evidence exists for a direct link between all three. Recent data shows that splicing components of the U2 small nuclear ribonucleic protein (snRNP) co-purify with Spt-Ada-Gcn5-acetyltransferase (SAGA), a highly conserved transcriptional co-activator and chromatin modifier. We hypothesize that SAGA binds with splicing components through a multi-protein binding surface with certain core components based on preliminary yeast two-hybrid data. …
Insights Into The Function Of The Fatc Domain Of Saccharomyces Cervisiae Tra1 Via Mutation And Suppressor Analysis, Samantha A. Pillon
Insights Into The Function Of The Fatc Domain Of Saccharomyces Cervisiae Tra1 Via Mutation And Suppressor Analysis, Samantha A. Pillon
Electronic Thesis and Dissertation Repository
The regulation of transcription is an important cellular function because it is the first step in gene regulation. In Saccharomyces cerevisiae, two protein complexes, SAGA and NuA4, act as regulators of transcription. A common protein shared between these two complexes, called Tra1, regulates transcriptional activation through its interaction with gene specific transcriptional activators. Tra1 is a member of the PIKK family of proteins, which are characterized by FAT, PI3K and FATC domains. The FATC domain encompasses the terminal 33-35 residues of the protein. Two mutations within the FATC domain, tra1-L3733A and tra1-F3744A, result in slow growth under stress …