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Rnp1p Plays a Role In P‐body Assembly in S. cerevisiae
Author(s) -
Mackay Katherine,
Segal Scott
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.711.28
Subject(s) - translation (biology) , stress granule , p bodies , psychological repression , messenger rna , microbiology and biotechnology , cytoplasm , chemistry , ribosome , translational regulation , biology , biochemistry , gene expression , gene , rna
Control of translation is an important response to physiological stress. Upon physiological stress, mRNA becomes unbound by ribosomes and shifts to cytoplasmic structures such as P‐bodies or stress granules (SG). P‐bodies and SG differ in that P‐bodies are thought to be sites of mRNA degradation, whereas SG are sites where mRNA are stored. In yeast, Pat1p, Dhh1p, and Sbp1p, nucleolin‐like factor are implicated in translational repression. Sbp1p also localizes to both P‐bodies and SG. Interestingly, SBP1 has a paralog, RNP1, whose function is not fully known. Sbp1p and Rnp1p both have two RRMs, but Rnp1 lacks the RRG box found in Sbp1p. Given the similarities between the two proteins, we determined whether Rnp1p plays a role in translational repression or P‐body/SG assembly. To determine Rnp1p role in these processes, rnp1Δ cells were stressed at high OD and P‐body assembly was ascertained. High OD exposure resulted in markedly reduced P‐body assembly as compared to control. Overexpression of Rnp1p in unstressed cells increased P‐body assembly. These results implicate Rnp1p in driving P‐body assembly or translational repression. To discern between these possibilities, further work will be done to localize Rnp1p, directly look at the translation of Rnp1p, and furthermore look at SG assembly.