Admission Procedure - Ph.D.

Friday Seminar by Ms. Rinchuila shimphrui


AG lab/ Friday/ May 4, 2018/ 3.30 pm/ HSPs-dependent stress granules dissembly and translationational recovery.
Category: Research
Posted by: bedineel

HSPs–dependent stress granules disassembly and translational recovery

 

Inhibition of protein synthesis during heat stress is one of the mechanisms employed by cells in order to limit the influx of newly synthesized proteins into the already overloaded proteome repair systems. This translational repression is usually followed by storage of the untranslated mRNAs along with various proteins into cytoplasmic foci known as messenger ribonucleoprotein (mRNP) granules. Processing bodies and stress granules (SGs) are two well-known cytosolic mRNPs. SGs are dynamic assembly consisting of untranslated mRNAs, RNA binding proteins, and components of translation initiation machinery. In plants, SGs have been associated with impaired stress tolerance and development. Several Heat Shock Proteins (HSPs) have been reported to be involved in SG assembly and disassembly. Recent studies have shown that HSP70/40 and HSP100 colocalize with SG and are critical for early translational recovery after heat stress.

 

References:

  1. Walters, R. W., Muhlrad, D., Garcia, J., & Parker, R. (2015). Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae. Rna21(9), 1660-1671.
  2. Cherkasov, V., Hofmann, S., Druffel-Augustin, S., Mogk, A., Tyedmers, J., Stoecklin, G., & Bukau, B. (2013). Coordination of translational control and protein homeostasis during severe heat stress. Current biology23(24), 2452-2462.
  3. Merret, R., Carpenier, M. C., Favory, J. J., Picart, C., Descombin, J., Bousquet-Antonelli, C., ... & Charng, Y. Y. (2017). Heat-shock protein HSP101 affects the release of ribosomal protein mRNAs for recovery after heat shock. Plant physiology, pp-00269.

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