@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},
doi = {10.1093/jxb/erab416},
volume = {},
user = {backofen},
pmid = {34499142},
pages = {},
number = {},
issn = {0022-0957},
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.}
}