RT Journal Article SR Electronic T1 HELZ directly interacts with CCR4–NOT and causes decay of bound mRNAs JF Life Science Alliance JO Life Sci. Alliance FD Life Science Alliance LLC SP e201900405 DO 10.26508/lsa.201900405 VO 2 IS 5 A1 Hanet, Aoife A1 Räsch, Felix A1 Weber, Ramona A1 Ruscica, Vincenzo A1 Fauser, Maria A1 Raisch, Tobias A1 Kuzuoğlu-Öztürk, Duygu A1 Chang, Chung-Te A1 Bhandari, Dipankar A1 Igreja, Cátia A1 Wohlbold, Lara YR 2019 UL http://www.life-science-alliance.org/content/2/5/e201900405.abstract AB 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.