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Steroid receptor RNA activator (SRA, or SRA1\; MIM 603819) is a complex RNA molecule containing multiple stable stem-loop structures that functions in coactivation of nuclear receptors. Additionally we are shipping and many more products for this protein.
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Although SLIRP is not involved in mediating bcl-2 (show BCL2 Antibodies) ability to protect from apoptosis and oxidative damage, bcl-2 (show BCL2 Antibodies) binds and stabilizes SLIRP protein and regulates mitochondrial mRNA levels. The BH4 domain of bcl-2 (show BCL2 Antibodies) has a role in maintaining this binding.
The LRPPRC (show LRPPRC Antibodies)/SLIRP complex suppressed 3' exonucleolytic mRNA degradation mediated by PNPase (show PNPT1 Antibodies) and SUV3 (show SUPV3L1 Antibodies).
LRPPRC exists in a high-molecular-weight complex, and it coimmunoprecipitates with SLIRP, a stem-loop RNA-binding protein.
Our data demonstrate that SLIRP modulates NR transactivation, suggest it may regulate mitochondrial function, and provide mechanistic insight into interactions between SRA (show SRA1 Antibodies), SLIRP, SRC-1 (show SRC Antibodies), and NCoR (show NCOR1 Antibodies).
SLIRP plays an essential role in maintaining mitochondrial-localized mRNA transcripts that encode OxPhos protein subunits.
both LRPPRC (show LRPPRC Antibodies) and SLIRP are required for maintaining mt-mRNA steady-state levels independent of their roles in stabilizing the other partner of the LRPPRC (show LRPPRC Antibodies)-SLIRP complex.
SLIRP regulates male fertility, wherein its loss results in asthenozoospermia associated with compromised sperm structure and mitochondrial morphology.
Steroid receptor RNA activator (SRA, or SRA1\; MIM 603819) is a complex RNA molecule containing multiple stable stem-loop structures that functions in coactivation of nuclear receptors. SLIRP interacts with stem-loop structure-7 of SRA (STR7) and modulates nuclear receptor transactivation (Hatchell et al., 2006
SRA stem-loop-interacting RNA-binding protein, mitochondrial
, chromosome 14 open reading frame 156