A unique HMG-box domain of mouse Maelstrom binds structured RNA but not double stranded DNA.

A unique HMG-box domain of mouse Maelstrom binds structured RNA but not double stranded DNA.

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Piwi-interacting piRNAs are a major and essential class of small RNAs in the animal germ cells with a prominent role in transposon control.Efficient piRNA biogenesis and function require a cohort of proteins conserved throughout the The use of plant waste to ensure the functioning of agricultural energy complexes animal kingdom.Here we studied Maelstrom (MAEL), which is essential for piRNA biogenesis and germ cell differentiation in flies and mice.MAEL contains a high mobility group (HMG)-box domain and a Maelstrom-specific domain with a presumptive RNase H-fold.

We employed a combination of sequence analyses, structural and biochemical approaches to evaluate and compare nucleic acid binding of mouse MAEL HMG-box to that of canonical HMG-box domain proteins (SRY and HMGB1a).MAEL HMG-box failed to bind double-stranded (ds)DNA but bound to structured RNA.We also identified important roles of a novel cluster of arginine residues in MAEL HMG-box in these interactions.Cumulatively, our results suggest that the MAEL HMG-box domain may contribute to MAEL function in selective processing of retrotransposon RNA into piRNAs.

In this regard, a cellular role of MAEL HMG-box domain is reminiscent of Digital marketing in Islamic perspective: A literature review that of HMGB1 as a sentinel of immunogenic nucleic acids in the innate immune response.