CK2 is an essential protein kinase implicated in various cellular processes. In 
this study, we address a potential role of this kinase in chromatin modulations 
associated with transcription. We found that CK2 depletion from yeast cells 
leads to replication-independent increase of histone H3K56 acetylation and 
global activation of H3 turnover in coding regions. This suggests a positive 
role of CK2 in maintenance/recycling of the histone H3/H4 tetramers during 
transcription. Interestingly, strand-specific RNA-seq analyses show that CK2 
inhibits global cryptic promoters driving both sense and antisense 
transcription. This further indicates a role of CK2 in the modulation of 
chromatin during transcription. Next, we showed that CK2 interacts with the 
major histone chaperone Spt6, and phosphorylates it in vivo and in vitro. CK2 
phosphorylation of Spt6 is required for its cellular levels, for the suppression 
of histone H3 turnover and for the inhibition of spurious transcription. 
Finally, we showed that CK2 and Spt6 phosphorylation sites are important to 
various transcriptional responses suggesting that cryptic intragenic and 
antisense transcript production are associated with a defective adaptation to 
environmental cues. Altogether, our data indicate that CK2 mediated 
phosphorylation of Spt6 regulates chromatin dynamics associated with 
transcription, and prevents aberrant transcription.