3PLV

Structure of Hub-1 protein in complex with Snu66 peptide (HINDII)

Summary for 3PLV

• Entry DOI: 10.2210/pdb3plv/pdb
• Related: 3PLU
• Descriptor: Ubiquitin-like modifier HUB1, 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component (3 entities in total)
• Functional Keywords: ubiquitin-like, peptide binding protein
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Nucleus: Q12420
• Total number of polymer chains: 2
• Total formula weight: 12723.55

Authors

Mishra, S.K.,Ammon, T.,Popowicz, G.M.,Krajewski, M.,Nagel, R.J.,Ares, M.,Holak, T.A.,Jentsch, S. (deposition date: 2010-11-15, release date: 2011-06-01, Last modification date: 2023-09-06)

Primary citation

Mishra, S.K.,Ammon, T.,Popowicz, G.M.,Krajewski, M.,Nagel, R.J.,Ares, M.,Holak, T.A.,Jentsch, S.
Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing.
Nature, 474:173-178, 2011

PubMed Abstract: Alternative splicing of pre-messenger RNAs diversifies gene products in eukaryotes and is guided by factors that enable spliceosomes to recognize particular splice sites. Here we report that alternative splicing of Saccharomyces cerevisiae SRC1 pre-mRNA is promoted by the conserved ubiquitin-like protein Hub1. Structural and biochemical data show that Hub1 binds non-covalently to a conserved element termed HIND, which is present in the spliceosomal protein Snu66 in yeast and mammals, and Prp38 in plants. Hub1 binding mildly alters spliceosomal protein interactions and barely affects general splicing in S. cerevisiae. However, spliceosomes that lack Hub1, or are defective in Hub1-HIND interaction, cannot use certain non-canonical 5' splice sites and are defective in alternative SRC1 splicing. Hub1 confers alternative splicing not only when bound to HIND, but also when experimentally fused to Snu66, Prp38, or even the core splicing factor Prp8. Our study indicates a novel mechanism for splice site utilization that is guided by non-covalent modification of the spliceosome by an unconventional ubiquitin-like modifier.

PubMed: 21614000
DOI: 10.1038/nature10143

Experimental method

X-RAY DIFFRACTION (1.9 Å)