Scott W. Stevens

Title: Assistant Professor


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Education: Ph.D: University of North Carolina at Chapel Hill
BS: University of Illinois at Urbana/Champaign
Postdoc.: California Institute of Technology, Pasadena, CA
Research: Processing and metabolism of RNA in eukaryotes
Office: MBB 2.448BA
Phone: 232-9303
E-mail: scott.stevens@mail.utexas.edu
Postal Address: Institute for Cellular and Molecular Biology
The University of Texas at Austin
1 University Sta. A4800
Austin, TX 78712
Courses taught:  
 

My laboratory is interested in the structure and function of ribonucleoproteins, in particular, the small nuclear ribonucleoproteins (snRNPs) involved in processing pre-mRNA.  There are a number of snRNPs in all eukaryotic cells, some highly conserved, others which seem to be specific to a group of organisms.  The splicing of pre-mRNA occurs in the context of the spliceosome, a 4-5 megadalton complex which contains the pre-mRNA, five snRNAs (U1, U2, U4, U5 and U6) and over 70 proteins.  There are many varieties of spliceosomal snRNPs in the eukaryotic nucleus.  In yeast, there are three abundant mono-snRNPs - the U1 snRNP, the U5 snRNP and the U6 snRNP.  There is a very small amount of a di-snRNP called U4/U6, more of a tri-snRNP called U4/U6•U5 and novel snRNPs I recently identified which participate directly in the splicing reaction.  These new snRNPs are termed the tetra-snRNP (U2•U4/U6•U5) and the penta-snRNP (U1•U2•U4/U6•U5) (See Stevens et al. Mol. Cell (2002)). 

Utilizing many techniques, such as yeast genetics, affinity chromatography, mass spectrometry, biochemistry and structural analysis, the overarching goal of this laboratory is to determine how ribonucleoproteins assemble, how they communicate with their substrate(s), how they undergo the drastic rearrangements they often do and how they disassemble to start the cycle over again. 

In addition to the ribonucleoproteins involved in pre-mRNA splicing, other snRNPs from yeast and human cells are being analyzed to determine their composition, assayed for function and their structures being determined by electron cryo-microscopy and X-Ray diffraction.


Selected Publications

2007

Proteomic analysis of in vivo assembled pre-mRNA splicing complexes expands the catalog of participating factorsNucleic Acids Res.
Chen, Y.-I., Moore, R.E., Ge, H.Y., Young, M.K., Lee, T.D. and S.W. Stevens (2007).    In press.

The pre-mRNA splicing mutant prp27-1 is a severe loss-of-function mutant of RAT1.
Gupton, L.D. and S.W. Stevens (2007).    Submitted

Induction of a profound immunodeficiency by modification of the pre-mRNA splicing factor SART1 (U4/U6•U5-110K).
Chen, Y.-I., Maika, S.D. and S.W. Stevens.  (2007).   Submitted.

Collaboration between two pre-mRNA splicing factors in the biogenesis and function of the tri-snRNP.
Roth, A.A. and S.W. Stevens.  (2007).   Submitted.

2006

Prp43p is a DEAH-box spliceosome disassembly factor essential for ribosome biogenesis.
Combs, D.J., Nagel, R.J., Ares, M. Jr. and S.W. Stevens (2006). Mol. Cell. Biol. 26; 523-534.

Epitope tagging of proteins at the native chromosomal loci of genes in mice and in cultured vertebrate cells.
Chen, Y.-I. Maika, S.D. and S.W. Stevens (2006). J. Mol. Biol. 361; 412-419.

2002

Pre-mRNA splicing in yeast: mechanisms, machinery and methods.
Stevens, S. W. and J. Abelson.  
Methods in Enzymology
 351: (2002) 200-220.

Composition and Functional Characterization of the Yeast Spliceosomal Penta-snRNP.
Stevens, S. W., Ryan, D. E., Ge H. Y., Moore R. E., Young M. K., Lee, T. D. and J. Abelson. 
Molecular
Cell  9: (2002) 41-54.

 

2001

Biochemical and genetic analyses of the U5, U6 and U4/U6•U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae.
Stevens, S. W., Ge H. Y., Moore R. E., Young M. K., Lee, T. D. and J. Abelson.
RNA 7: (2001) 1543-1553.
 

1999

Analysis of low-abundance RNPs from yeast by affinity chromatography and mass spectrometry microsequencing. 
Stevens, S. W. 
Methods in Enzymology
318: (1999) 385-398.

Purification of the yeast U4/U6•U5 snRNP and identification of its associated proteins. 
Stevens, S. W. and J. Abelson. 
Proc. Natl. Acad. Sci. U.S.A.
96: (1999) 7226-7231.
 


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