HELZ directly interacts with CCR4-NOT and causes decay of bound mRNAs

Aoife Hanet, Felix Räsch, Ramona Weber, Vincenzo Ruscica, Maria Fauser, Tobias Raisch, Duygu Kuzuoglu-Öztürk, Chung Te Chang, Dipankar Bhandari, Cátia Igreja*, Lara Wohlbold

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Eukaryotic superfamily (SF) 1 helicases have been implicated in various aspects of RNA metabolism, including transcription, processing, translation, and degradation. Nevertheless, until now, most human SF1 helicases remain poorly understood. Here, we have functionally and biochemically characterized the role of a putative SF1 helicase termed “helicase with zinc-finger,” or HELZ. We discovered that HELZ associates with various mRNA decay factors, including components of the carbon catabolite repressor 4-negative on TATA box (CCR4-NOT) deadenylase complex in human and Drosophila melanogaster cells. The interaction between HELZ and the CCR4-NOT complex is direct and mediated by extended low-complexity regions in the C-terminal part of the protein. We further reveal that HELZ requires the deadenylase complex to mediate translational repression and decapping-dependent mRNA decay. Finally, transcriptome-wide analysis of Helz-null cells suggests that HELZ has a role in the regulation of the expression of genes associated with the development of the nervous system.

Original languageEnglish
Article number201900405
JournalLife Science Alliance
Issue number5
StatePublished - 2019


Dive into the research topics of 'HELZ directly interacts with CCR4-NOT and causes decay of bound mRNAs'. Together they form a unique fingerprint.

Cite this