Translation initiation factor eIF4E forms eIF4E-eIF4G complex
at the 5’ cap of mRNA. This interaction can be inhibited
by the family of 4E-binding proteins (4E-BP). In yeast
Saccharomyces cerevisiae, two 4E-BPs, Caf20 and Eap1, compete
with eIF4G for binding to eIF4E via the shared conserved
interaction motif. In order to investigate the roles of Caf20
in gene-specific translational regulation and the formation
of mRNA granules (P-bodies), we introduced substitution
mutations, caf20-Y4A or caf20-L9A, in the eIF4E-binding
motif for CAF20. Overexpression of the wild-type CAF20
showed an increased protein level of Ste12 transcription factor
as well as highly developed P-body formation. However,
4E-binding site mutations of CAF20 led to a reduced number
of P-body foci and decreased levels of Ste12 protein. The
phenotypes of the caf20 deletion mutation were also analyzed,
and we suggest that Caf20 plays a critical role in Ste12 protein
expression and in the control of P-body formation.
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Functional association of Loc1 and Puf6 with RNA helicase Dhh1 in translational regulation of Saccharomyces cerevisiae Ste12 Daehee Jung, Jong Seok Seo, Jayoung Nam, Jinmi Kim, Enrico Baruffini PLOS ONE.2019; 14(7): e0220137. CrossRef
Dhh1 and Dhh1 homologues (RCK/p54/DDX6) are mem-bers of the DEAD-box protein family of RNA helicases. These proteins display conserved sequence motifs for ATPase and RNA binding activities. Dhh1 is a component of the P-bodies (processing bodies) of mRNA granules and functions as an mRNA decapping activator in Saccharomyces cerevisiae. Dhh1 also contributes to gene-specific regulation during yeast mating. The dhh1 deletion mutation results in a significant decrease in the expression of Ste12, a mating-specific trans-cription factor, showing severe mating defects. Here, we in-troduced amino-acid substitution mutations in the ATPase and RNA binding domains of Dhh1 and also constructed a deletion of 79 amino acids at the Q/P-rich C-terminal region. The mutations in ATPase A and B motif (K96R, D195A) and C-terminus deletion showed reduced levels of mating effi-ciency as well as Ste12 protein expression. The Q/P-rich C- terminal region of Dhh1 was dispensable for growth at non- permissive temperature 37°C but appeared to play an im-portant role in regulating the Ste12 protein expression and mating processes. The P-body accumulation induced by treatment with α-mating factor required ATPase, RNA-bind-ing and the Q/P-rich C-terminal domains of Dhh1.
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Fus3 and Tpk2 protein kinases regulate the phosphorylation-dependent functions of RNA helicase Dhh1 in yeast mating and Ste12 protein expression Jaehee Hwang, Daehee Jung, Jinmi Kim Journal of Microbiology.2022; 60(8): 843. CrossRef
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Functional association of Loc1 and Puf6 with RNA helicase Dhh1 in translational regulation of Saccharomyces cerevisiae Ste12 Daehee Jung, Jong Seok Seo, Jayoung Nam, Jinmi Kim, Enrico Baruffini PLOS ONE.2019; 14(7): e0220137. CrossRef
Roles of eIF4E-binding protein Caf20 in Ste12 translation and P-body formation in yeast Kiyoung Park, Yu-Seon Lee, Daehee Jung, Jinmi Kim Journal of Microbiology.2018; 56(10): 744. CrossRef