Recent studies show that nuclear RNase P is linked to chromatin structure and function. Thus, variants of this ribonucleoprotein (RNP) complex bind to chromatin of small noncoding RNA genes; integrate into initiation complexes of RNA polymerase (Pol) III; repress histone H3.3 nucleosome deposition; control tRNA and PIWI-interacting RNA (piRNA) gene clusters for genome defense; and respond to Werner syndrome helicase (WRN)-related replication stress and DNA double-strand breaks (DSBs). Likewise, the related RNase MRP and RMRP-TERT (telomerase reverse transcriptase) are implicated in RNA-dependent RNA polymerization for chromatin silencing, whereas the telomerase carries out RNA-dependent DNA polymerization for telomere lengthening. Remarkably, the four RNPs share several protein subunits, including two Alba-like chromatin proteins that possess DEAD-like and ATPase motifs found in chromatin modifiers and remodelers. Based on available data, RNase P and related RNPs act in transition processes of DNA to RNA and vice versa and connect these processes to genome preservation, including replication, DNA repair, and chromatin remodeling.

最近的研究表明，核RNase P与染色质的结构和功能有关。因此，这种核糖核蛋白（RNP）复合物的变体与小的非编码RNA基因的染色质结合。整合入RNA聚合酶（Pol）III的起始复合物中；抑制组蛋白H3.3核小体沉积；控制用于基因组防御的tRNA和PIWI相互作用RNA（piRNA）基因簇；并响应与Werner综合征解旋酶（WRN）相关的复制压力和DNA双链断裂（DSB）。同样，相关的RNase MRP和RMRP-TERT（端粒酶逆转录酶）也参与了染色质沉默的RNA依赖RNA聚合，而端粒酶则进行了RNA依赖的DNA聚合以延长端粒。值得注意的是，四个RNP共有几个蛋白亚基，包括两个在染色质修饰剂和重塑剂中具有DEAD-like和ATPase基序的Alba-like染色质蛋白。根据现有数据，RNase P和相关的RNP在DNA向RNA的转变过程中起作用，反之亦然，并将这些过程与基因组保存联系起来，包括复制，DNA修复和染色质重塑。