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Stem-loop binding protein (SLBP) is a key regulatory protein that binds with high specificity to the conserved stem-loop structure at the 3′ end of replication-dependent histone mRNAs[1][2][3][4][5]. Unlike most mRNAs, histone mRNAs lack polyadenylation and rely on SLBP for post-transcriptional processing, export from the nucleus, stability, and translation. SLBP participates in the cleavage of histone pre-mRNAs through interactions with the U7 snRNP complex, promoting efficient and timely histone gene expression during DNA replication. The RNA-binding domain of SLBP recognizes the overall shape of the stem-loop and specific base pairs, stabilizing mRNA structure and facilitating recruitment of processing factors. SLBP levels and activity are tightly regulated during the cell cycle and play a critical role in coupling histone synthesis to DNA replication in eukaryotic cells[1][2][3][4][5]. Abnormal SLBP function can impair cell proliferation and differentiation, and has been implicated experimentally in certain developmental and proliferative disorders[3][4].
None established for drugs targeting SLBP
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