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Investigating Functional Roles of RPS3 in RNA Damage
Author(s) -
Limoncelli Kelly,
Merrikh Christopher,
Rhind Nicholas,
Korostelev Andrei,
Moore Melissa
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.711.17
Subject(s) - rna , ribosome , messenger rna , microbiology and biotechnology , dna damage , biology , ribosomal rna , ribosomal protein , dna , genetics , gene
Damaging agents, such as UV‐rays and reactive oxygen species, compromise both DNA and RNA molecules. Yet while response to DNA damage has received considerable attention, how cells recognize and deal with damaged RNA remains poorly understood. No‐go decay (NGD) and nonfunctional 18S rRNA decay (18S NRD) are quality control mechanisms that recognize stalled ribosomes and stimulate degradation of associated aberrant RNAs. Both mechanisms require termination homologs Dom34 and Hbs1 for dissociating stalled ribosomal subunits 1 . Additionally, we have evidence suggesting 18S NRD requires ASC1 , a WD40‐repeat protein known to mediate destabilization of peptides associated with stalled ribosomes 2 . Since damaged bases within mRNA coding regions result in stalled ribosomes, we wondered if a translation‐dependent surveillance pathway exists for damaged mRNA molecules. Ribosomal protein S3 ( RPS3 ), which forms part of the mRNA entrance channel, has been implicated as an endonuclease for abasic and UV‐irradiated dsDNA 3 . Furthermore, Rps3 structurally interacts with Asc1 and Hbs1, suggesting a possible role in RNA quality control. To investigate whether RPS3 functions in processing damaged RNA, we are screening Saccharomyces cerevisiae rps3 mutants that exhibit wild‐type growth rates under normal conditions, yet increased sensitivity toward damaging agents.