TXNL4A contains a thioredoxin-like fold, which is a characteristic structural motif found in thioredoxin proteins . This fold allows TXNL4A to interact with multiple proteins, including the polyglutamine tract-binding protein 1 (PQBP1) . The primary function of TXNL4A is to participate in the assembly of the spliceosome, a complex responsible for removing introns from pre-mRNA .
TXNL4A plays a crucial role in the processing of capped intron-containing pre-mRNA and is involved in the mRNA splicing minor pathway . It is a component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes, which are essential for the formation of the spliceosome . The protein’s interactions and functions are vital for the accurate and efficient splicing of pre-mRNA, ensuring proper gene expression and cellular function .
Mutations in the TXNL4A gene have been associated with Burn-McKeown syndrome, a rare genetic disorder characterized by craniofacial dysmorphisms, cardiac defects, hearing loss, and bilateral choanal atresia . Additionally, TXNL4A is linked to Developmental and Epileptic Encephalopathy 7, highlighting its importance in neurological development and function .
Recombinant forms of TXNL4A are used in research to study its structure, function, and interactions with other proteins. Understanding the role of TXNL4A in pre-mRNA splicing and its involvement in genetic disorders can provide insights into potential therapeutic targets for related diseases.