E-MTAB-2028 - RNA-seq of coding RNA from Apsergillus fumigatus ( AfS28, dakuA::ptrA) with or without endoplasmic recticulum stress induced by dithothreitol and tunicamycin
Last updated on 14 November 2013, released on 13 January 2014
The unfolded protein response (UPR) is a network of intracellular signaling pathways that supports the ability of the secretory pathway to maintain equilibrium between the load of proteins entering the endoplasmic reticulum (ER) and the protein folding capacity of the ER lumen. Current evidence suggests that human pathogenic fungi rely heavily on this pathway for virulence, but there is limited understanding of the mechanisms involved. The best known functional output of the UPR is transcriptional upregulation of mRNAs involved in ER homeostasis. However, this does not take into account mechanisms of translational regulation that involve differential recruitment of mRNAs to ribosomes. In this study, a global analysis of transcript-specific translational regulation was performed in the pathogenic mold Aspergillus fumigatus to determine the nature and scope of the translational response to ER stress.
RNA-seq of coding RNA, dose response
Polysome profiling reveals broad translatome remodeling during endoplasmic reticulum (ER) stress in the pathogenic fungus Aspergillus fumigatus. Karthik Krishnan, Zhaowei Ren, William C. Nierman, Long Jason Lu, David S. Askew.