Cargando…
Structure-function analysis of the 5′ end of yeast U1 snRNA highlights genetic interactions with the Msl5•Mud2 branchpoint-binding complex and other spliceosome assembly factors
Yeast pre-mRNA splicing initiates via formation of a complex comprising U1 snRNP bound at the 5′ splice site (5′SS) and the Msl5•Mud2 heterodimer engaged at the branchpoint (BP). Here, we present a mutational analysis of the U1 snRNA, which shows that although enlarging the 5′ leader between the TMG...
Autores principales: | Schwer, Beate, Chang, Jonathan, Shuman, Stewart |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753624/ https://www.ncbi.nlm.nih.gov/pubmed/23754852 http://dx.doi.org/10.1093/nar/gkt490 |
Ejemplares similares
-
Structure-function analysis of the Yhc1 subunit of yeast U1 snRNP and genetic interactions of Yhc1 with Mud2, Nam8, Mud1, Tgs1, U1 snRNA, SmD3 and Prp28
por: Schwer, Beate, et al.
Publicado: (2014) -
Structure–function analysis and genetic interactions of the yeast branchpoint binding protein Msl5
por: Chang, Jonathan, et al.
Publicado: (2012) -
Structural basis for recognition of intron branchpoint RNA by yeast Msl5 and selective effects of interfacial mutations on splicing of yeast pre-mRNAs
por: Jacewicz, Agata, et al.
Publicado: (2015) -
The Lsm2-8 complex determines nuclear localization of the spliceosomal U6 snRNA
por: Spiller, Michael P., et al.
Publicado: (2007) -
Composition of yeast snRNPs and snoRNPs in the absence of trimethylguanosine caps reveals nuclear cap binding protein as a gained U1 component implicated in the cold-sensitivity of tgs1Δ cells
por: Schwer, Beate, et al.
Publicado: (2011)