Faculty, Staff and Student Publications
Language
English
Publication Date
1-2-2024
Journal
Biochemistry
DOI
10.1021/acs.biochem.3c00401
PMID
38085597
PMCID
PMC10984559
PubMedCentral® Posted Date
April 2024
PubMedCentral® Full Text Version
Author MSS
Abstract
Mtr4 is an essential RNA helicase involved in nuclear RNA processing and degradation and is a member of the Ski2-like helicase family. Ski2-like helicases share a common core architecture that includes two RecA-like domains, a winged helix, and a helical bundle (HB) domain. In Mtr4, a short C-terminal tail immediately follows the HB domain and is positioned at the interface of the RecA-like domains. The tail ends with a SLYΦ sequence motif that is highly conserved in a subset of Ski2-like helicases. Here, we show that this sequence is critical for Mtr4 function. Mutations in the C-terminus result in decreased RNA unwinding activity. Mtr4 is a key activator of the RNA exosome complex, and mutations in the SLYΦ motif produce a slow growth phenotype when combined with a partial exosome defect in
Keywords
Exosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Exosome Multienzyme Ribonuclease Complex, DEAD-box RNA Helicases, RNA Helicases, DNA Helicases
Published Open-Access
yes
Recommended Citation
Yim, Matthew K; Stuart, Catherine J; Pond, Markell I; et al., "Conserved Residues at the Mtr4 C-Terminus Coordinate Helicase Activity and Exosome Interactions" (2024). Faculty, Staff and Student Publications. 1337.
https://digitalcommons.library.tmc.edu/uthmed_docs/1337