The HIV-1 Rev Activation Domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
The Spinal Muscular Atrophy Disease Gene Product, SMN, and Its Associated Protein SIP1 Are in a Complex with Spliceosomal snRNP Proteins
Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing.
The U7-specific Lsm11 protein not only specifies the assembly of the U7 Sm core but also fulfills an important role in U7 snRNP-mediated histone mRNA processing.
The SMN–SIP1 Complex Has an Essential Role in Spliceosomal snRNP Biogenesis
A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs
- G. Meister, D. Bühler, R. Pillai, F. Lottspeich, U. Fischer
- BiologyNature Cell Biology
- 1 November 2001
It is shown that assembly of U1 snRNP depends on ATP, the first direct evidence that a complex containing SMN and Gemin2 mediates the active assembly of spliceosomal U snRNPs.
Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
HIV‐1 infection of non‐dividing cells: evidence that the amino‐terminal basic region of the viral matrix protein is important for Gag processing but not for post‐entry nuclear import
It is found that disruption of this region (26KK→TT) reduces the rate at which the viral Gag polyprotein (p55Gag) is post‐translationally processed by the viral protease.
SMN Tudor domain structure and its interaction with the Sm proteins
- Philipp Selenko, R. Sprangers, G. Stier, D. Bühler, U. Fischer, M. Sattler
- Biology, ChemistryNature Structural Biology
The three-dimensional structure of the Tudor domain of human SMN is determined and it is shown that a conserved negatively charged surface that is shown to interact with the C-terminal Arg and Gly-rich tails of Sm proteins.
Interaction of the Human Immunodeficiency Virus Type 1 Vpr Protein with the Nuclear Pore Complex
These findings not only demonstrate that Vpr harbors a bona fide NLS but also raise the possibility that one (or more) of Vpr’s functions may take place at the NPC.
Reduced U snRNP assembly causes motor axon degeneration in an animal model for spinal muscular atrophy.
Gen silencing is used to assess the effect of SMN protein deficiency on U snRNP metabolism in living cells and organisms and suggests that motoneuron degeneration in SMA patients is a direct consequence of impaired production of U snRNPs.