RT Journal Article
SR Electronic
T1 Multiplexed mRNA assembly into ribonucleoprotein particles plays an operon-like role in the control of yeast cell physiology
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.06.28.175851
DO 10.1101/2020.06.28.175851
A1 Nair, Rohini R.
A1 Zabezhinsky, Dimitry
A1 Gelin-Licht, Rita
A1 Haas, Brian
A1 Dyhr, Michael C.A.
A1 Sperber, Hannah S.
A1 Nusbaum, Chad
A1 Gerst, Jeffrey E.
YR 2020
UL http://biorxiv.org/content/early/2020/06/28/2020.06.28.175851.abstract
AB Prokaryotes utilize polycistronic messages (operons) to co-translate proteins involved in the same biological process. Whether eukaryotes achieve similar regulation by selectively assembling monocistronic messages derived from different chromosomes is unclear. We employed transcript-specific RNA pulldowns and RNA-seq/RT-PCR to identify mRNAs that co-precipitate into ribonucleoprotein (RNP) particles in yeast. Consistent with the hypothesis of eukaryotic RNA operons, mRNAs encoding components of the mating pathway, heat shock proteins, and mitochondrial outer membrane proteins multiplex in trans to form discrete mRNP particles, termed transperons. Chromatin-capture experiments reveal that genes encoding multiplexed mRNAs physically interact, thus, RNA assembly may result from co-regulated gene expression. Transperon assembly and function depends upon H4 histones and their depletion leads to defects in RNA multiplexing, resulting in decreased pheromone responsiveness and mating, and increased heat shock sensitivity. We propose that intergenic associations and non-canonical H4 histone functions contribute to transperon formation in eukaryotic cells to regulate cell physiology.Competing Interest StatementThe authors have declared no competing interest.