English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

The human LINE‐1/L1 ORF2 protein is a multifunctional enzyme which plays a vital role in the life cycle of the human L1 retrotransposon. The protein consists of an endonuclease domain, followed by a central reverse transcriptase domain and a carboxy‐terminal C‐domain with unknown function. Here, we explore the nucleic acid binding properties of the 180‐amino acid carboxy‐terminal segment (CTS) of the human L1 ORF2p  in vitro . In a series of experiments involving gel shift assay, we demonstrate that the CTS of L1 ORF2p binds RNA in non‐sequence‐specific manner. Finally, we report that mutations destroying the putative Zn‐knuckle structure of the protein do not significantly affect the level of RNA binding and discuss the possible functional role of the CTS in L1 retrotransposition.

The carboxy‐terminal segment of the human LINE‐1 ORF2 protein is involved in RNA binding