@Article{Migur_Heyl_Fuss-The_tempe_DEAD-2021,
  author =	 {Migur, Anzhela and Heyl, Florian and Fuss, Janina and 
                  Srikumar, Afshan and Huettel, Bruno and Steglich, Claudia 
                  and Prakash, Jogadhenu S. S. and Reinhardt, Richard and 
                  Backofen, Rolf and Owttrim, George W. and Hess, Wolfgang R.},
  title =	 {The temperature-regulated {DEAD}-box {RNA} helicase {CrhR} 
                  interactome: {Autoregulation} and photosynthesis-related 
                  transcripts},
  journal =	 {J Exp Bot},
  year =	 {2021},
  volume =	 {},
  number =	 {},
  pages =	 {},
  user =	 {backofen},
  pmid =	 {34499142},
  doi = 	 {10.1093/jxb/erab416},
  issn = 	 {0022-0957},
  issn = 	 {1460-2431},
  abstract =	 {RNA helicases play crucial functions in RNA biology. In 
                  plants, RNA helicases are encoded by large gene families, 
                  performing roles in abiotic stress responses, development, 
                  the post-transcriptional regulation of gene expression as 
                  well as house-keeping functions. Several of these RNA 
                  helicases are targeted to the organelles, mitochondria and 
                  chloroplasts. Cyanobacteria are the direct evolutionary 
                  ancestors of plant chloroplasts. The cyanobacterium 
                  Synechocystis 6803 encodes a single DEAD-box RNA helicase, 
                  CrhR, that is induced by a range of abiotic stresses, 
                  including low temperature. Though the DeltacrhR mutant 
                  exhibits a severe cold-sensitive phenotype, the 
                  physiological function(s) performed by CrhR have not been 
                  described. To identify transcripts interacting with CrhR, we 
                  performed RNA co-immunoprecipitation with extracts from a 
                  Synechocystis crhR deletion mutant expressing the 
                  FLAG-tagged native CrhR or a K57A mutated version with an 
                  anticipated enhanced RNA binding. The composition of the 
                  interactome was strikingly biased towards 
                  photosynthesis-associated and redox-controlled transcripts. 
                  A transcript highly enriched in all experiments was the crhR 
                  mRNA, suggesting an auto-regulatory molecular mechanism. The 
                  identified interactome explains the described physiological 
                  role of CrhR in response to the redox poise of the 
                  photosynthetic electron transport chain and characterizes 
                  CrhR as an enzyme with a diverse range of transcripts as 
                  molecular targets.}
}