LOTUS domain is a novel class of G-rich and G-quadruplex RNA binding domain

Deqiang Ding, Chao Wei, Kunzhe Dong, Jiali Liu, Alexander Stanton, Chao Xu, Jinrong Min, Jian Hu, Chen Chen

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


LOTUS domains are helix-turn-helix protein folds identified in essential germline proteins and are conserved in prokaryotes and eukaryotes. Despite originally predicted as an RNA binding domain, its molecular binding activity towards RNA and protein is controversial. In particular, the most conserved binding property for the LOTUS domain family remains unknown. Here, we uncovered an unexpected specific interaction of LOTUS domains with G-rich RNA sequences. Intriguingly, LOTUS domains exhibit high affinity to RNA G-quadruplex tertiary structures implicated in diverse cellular processes including piRNA biogenesis. This novel LOTUS domain-RNA interaction is conserved in bacteria, plants and animals, comprising the most ancient binding feature of the LOTUS domain family. By contrast, LOTUS domains do not preferentially interact with DNA G-quadruplexes. We further show that a subset of LOTUS domains display both RNA and protein binding activities. These findings identify the LOTUS domain as a specialized RNA binding domain across phyla and underscore the molecular mechanism underlying the function of LOTUS domain-containing proteins in RNA metabolism and regulation.

Original languageEnglish (US)
Pages (from-to)9262-9272
Number of pages11
JournalNucleic Acids Research
Issue number16
StatePublished - Sep 18 2020
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


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