MGSSHHHHHH SSGLVPRGSH MLPLSLLKTA QNHPMLVELK NGETYNGHLV SCDNWMNINL REVICTSRDG DKFWRMPECY IRGSTIKYLR IPDEIIDMVK EEVVAKGRGR GGLQQQKQQK GRGMGGAGRG VFGGRGRGGI PGTGRGQPEK KPGRQAGKQ.
LSM4 is part of the heptameric LSM2-8 complex, which binds specifically to the 3’-terminal oligo(U) tract of U6 small nuclear RNA (snRNA). This binding is essential for the stability and function of U6 snRNA, a critical component of the spliceosome . The spliceosome is a complex molecular machine responsible for removing introns from pre-mRNA, a process known as splicing .
The LSM2-8 complex, including LSM4, is involved in the formation of the U4/U6-U5 tri-snRNP complex, which is a key component of the spliceosome assembly. This complex plays a significant role in the pre-mRNA splicing process by mediating the formation of the spliceosome’s catalytic core .
LSM4 is associated with several important biological pathways, including:
The recombinant form of LSM4, known as “LSM4 Homolog, U6 Small Nuclear RNA Associated (Human Recombinant),” is used in various research applications to study its function and role in RNA metabolism. This recombinant protein is produced using recombinant DNA technology, which allows for the expression of the human LSM4 gene in a host organism, such as bacteria or yeast .
Researchers use this recombinant protein to investigate the molecular mechanisms underlying RNA processing and degradation, as well as to develop potential therapeutic strategies for diseases associated with LSM4 dysfunction .