Show simple item record

dc.contributor.authorWilkinson, Caroline R M
dc.contributor.authorDittmar, Gunnar A G
dc.contributor.authorOhi, Melanie D
dc.contributor.authorUetz, Peter
dc.contributor.authorJones, Nic
dc.contributor.authorFinley, Daniel
dc.date.accessioned2009-08-24T16:17:39Z
dc.date.available2009-08-24T16:17:39Z
dc.date.issued2004-12-29
dc.identifier.citationUbiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast. 2004, 14 (24):2283-8 Curr. Biol.en
dc.identifier.issn0960-9822
dc.identifier.pmid15620657
dc.identifier.doi10.1016/j.cub.2004.11.058
dc.identifier.urihttp://hdl.handle.net/10541/78368
dc.description.abstractHub1/Ubl5 is a member of the family of ubiquitin-like proteins (UBLs). The tertiary structure of Hub1 is similar to that of ubiquitin; however, it differs from known modifiers in that there is no conserved glycine residue near the C terminus which, in ubiquitin and UBLs, is required for covalent modification of target proteins. Instead, there is a conserved dityrosine motif proximal to the terminal nonconserved amino acid. In S. cerevisiae, high molecular weight adducts can be formed in vivo from Hub1, but the structure of these adducts is not known, and they could be either covalent or noncovalent. The budding yeast HUB1 gene is not essential, but Delta hub1 mutants display defects in mating. Here, we report that fission yeast hub1 is an essential gene, whose loss results in cell cycle defects and inefficient pre-mRNA splicing. A screen for Hub1 interactors identified Snu66, a component of the U4/U6.U5 tri-snRNP splicing complex. Furthermore, overexpression of Snu66 suppresses the lethality of a hub1ts mutant. In cells lacking functional hub1, the nuclear localization of Snu66 is disrupted, suggesting that an important role for Hub1 is the correct subcellular targeting of Snu66, although our data suggest that Hub1 is likely to perform other roles in splicing as well.
dc.language.isoenen
dc.subject.meshCell Cycle
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshFlow Cytometry
dc.subject.meshGenes, Essential
dc.subject.meshMicroscopy, Fluorescence
dc.subject.meshMutation
dc.subject.meshOligonucleotides
dc.subject.meshProtein Transport
dc.subject.meshRNA Splicing
dc.subject.meshReverse Transcriptase Polymerase Chain Reaction
dc.subject.meshRibonucleoproteins, Small Nuclear
dc.subject.meshSchizosaccharomyces
dc.subject.meshSchizosaccharomyces pombe Proteins
dc.subject.meshTwo-Hybrid System Techniques
dc.subject.meshUbiquitin-Protein Ligase Complexes
dc.titleUbiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast.en
dc.typeArticleen
dc.contributor.departmentDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. cwilkinson@picr.man.ac.uken
dc.identifier.journalCurrent Biologyen
html.description.abstractHub1/Ubl5 is a member of the family of ubiquitin-like proteins (UBLs). The tertiary structure of Hub1 is similar to that of ubiquitin; however, it differs from known modifiers in that there is no conserved glycine residue near the C terminus which, in ubiquitin and UBLs, is required for covalent modification of target proteins. Instead, there is a conserved dityrosine motif proximal to the terminal nonconserved amino acid. In S. cerevisiae, high molecular weight adducts can be formed in vivo from Hub1, but the structure of these adducts is not known, and they could be either covalent or noncovalent. The budding yeast HUB1 gene is not essential, but Delta hub1 mutants display defects in mating. Here, we report that fission yeast hub1 is an essential gene, whose loss results in cell cycle defects and inefficient pre-mRNA splicing. A screen for Hub1 interactors identified Snu66, a component of the U4/U6.U5 tri-snRNP splicing complex. Furthermore, overexpression of Snu66 suppresses the lethality of a hub1ts mutant. In cells lacking functional hub1, the nuclear localization of Snu66 is disrupted, suggesting that an important role for Hub1 is the correct subcellular targeting of Snu66, although our data suggest that Hub1 is likely to perform other roles in splicing as well.


Files in this item

This item appears in the following Collection(s)

Show simple item record