Premium
Unrip is a component of SMN complexes active in snRNP assembly
Author(s) -
Carissimi Claudia,
Baccon Jennifer,
Straccia Marco,
Chiarella Pieranna,
Maiolica Alessio,
Sawyer Alan,
Rappsilber Juri,
Pellizzoni Livio
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.034
Subject(s) - snrnp , small nuclear ribonucleoprotein , ribonucleoprotein , microbiology and biotechnology , biogenesis , spinal muscular atrophy , biology , cajal body , spliceosome , chemistry , rna splicing , rna , biochemistry , gene
A macromolecular complex containing survival of motor neurons (SMN), the spinal muscular atrophy protein, and Gemin2–7 interacts with Sm proteins and snRNAs to carry out the assembly of these components into spliceosomal small nuclear ribonucleoproteins (snRNPs). Here we report the characterization of unr‐interacting protein (unrip), a GH‐WD protein of unknown function, as a component of the SMN complex that interacts directly with Gemin6 and Gemin7. Unrip also binds a subset of Sm proteins, and unrip‐containing SMN complexes are necessary and sufficient to mediate the assembly of spliceosomal snRNPs. These results demonstrate that unrip functions in the pathway of snRNP biogenesis and is a marker of cellular SMN complexes active in snRNP assembly.