The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding.

ABSTRACT:

Background

Vertebrates have one Dicer ortholog that generates both microRNAs (miRNAs) and small interfering RNAs (siRNAs), in contrast to the multiple Dicer-like proteins found in flies and plants. Here, we focus on the functions of the human Dicer (hDicer) helicase domain. The helicase domain of hDicer is known to recognize pre-miRNA substrates through interactions with their apical loop regions. Besides interacting with canonical substrates, the hDicer helicase domain has also been suggested to bind many different cellular RNAs; however, a comprehensive study of the biochemical activities and substrate specificity of the hDicer helicase domain towards different nucleic acids has yet to be undertaken.

Results

Here, we reveal that full-length hDicer, through its helicase dom

SUBMITTER: Ciechanowska K 

PROVIDER: S-EPMC11658451 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature