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Biochemistry, Biophysics, and Structural Biology Commons™
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Articles 1 - 3 of 3
Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
The C. Elegans Heterochronic Gene Lin-46 Affects Developmental Timing At Two Larval Stages And Encodes A Relative Of The Scaffolding Protein Gephyrin, A. S.-R. Pepper, Jill E. Mccane, Kevin Kemper, Dennis Au Yeung, Rosalind C. Lee, Victor Ambros, Eric G. Moss
The C. Elegans Heterochronic Gene Lin-46 Affects Developmental Timing At Two Larval Stages And Encodes A Relative Of The Scaffolding Protein Gephyrin, A. S.-R. Pepper, Jill E. Mccane, Kevin Kemper, Dennis Au Yeung, Rosalind C. Lee, Victor Ambros, Eric G. Moss
Dartmouth Scholarship
The succession of developmental events in the C. elegans larva is governed by the heterochronic genes. When mutated, these genes cause either precocious or retarded developmental phenotypes, in which stage-specific patterns of cell division and differentiation are either skipped or reiterated, respectively. We identified a new heterochronic gene, lin-46, from mutations that suppress the precocious phenotypes caused by mutations in the heterochronic genes lin-14 and lin-28. lin-46 mutants on their own display retarded phenotypes in which cell division patterns are reiterated and differentiation is prevented in certain cell lineages. Our analysis indicates that lin-46 acts at a step immediately downstream …
Mer1p Is A Modular Splicing Factor Whose Function Depends On The Conserved U2 Snrnp Protein Snu17p, Marc Spingola, Javier Armisen, Manuel Ares
Mer1p Is A Modular Splicing Factor Whose Function Depends On The Conserved U2 Snrnp Protein Snu17p, Marc Spingola, Javier Armisen, Manuel Ares
Biology Department Faculty Works
Mer1p activates the splicing of at least three pre‐mRNAs (AMA1, MER2, MER3) during meiosis in the yeast Saccharomyces cerevisiae. We demonstrate that enhancer recognition by Mer1p is separable from Mer1p splicing activation. The C‐terminal KH‐type RNA‐binding domain of Mer1p recognizes introns that contain the Mer1p splicing enhancer, while the N‐terminal domain interacts with the spliceosome and activates splicing. Prior studies have implicated the U1 snRNP and recognition of the 5′ splice site as key elements in Mer1p‐activated splicing. We provide new evidence that Mer1p may also function at later steps of spliceosome assembly. First, Mer1p can activate splicing of introns …
Mer1p Is A Modular Splicing Factor Whose Function Depends On The Conserved U2 Snrnp Protein Snu17p, Marc Spingola, Javier Armisen, Manuel Ares
Mer1p Is A Modular Splicing Factor Whose Function Depends On The Conserved U2 Snrnp Protein Snu17p, Marc Spingola, Javier Armisen, Manuel Ares
Marc Spingola