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.