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Transcriptional kinases

Conducting the CTD orchestra

Nature Chemical Biology volume 15, pages 97–98 (2019)Cite this article

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The carboxyl-terminal domain (CTD) of RNA polymerase II (Pol II) is post-translationally modified during gene expression. A recent study has identified a CTD kinase, Hrr25, that regulates the termination of noncoding RNA genes by recruiting Rtt103, a key termination factor.

In 1985, an unusual extension in the 3′ gene coding for the largest subunit of the Pol II was identified as a tandem repetition of seven residues, Y1S2P3T4S5P6S7, known today as the CTD1,2. At the time, the abundance of potential phosphorylation sites in the CTD was already noted, although the functional relevance of these sites was not known. Subsequent studies have revealed some ‘writers’ and ‘readers’ of the complex code that composed CTD post-translational modifications that have important implications in gene expression3. In this issue, Nemec et al.4 identify 11 kinases that significantly phosphorylate threonine 4 (Thr4) in vitro and reveal that the inhibition of one of these kinases, Hrr25, leads to bypassing the termination site of several snoRNA, a peculiar class of noncoding RNAs (ncRNAs).

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Fig. 1: CTD phosphorylation during transcription initiation, elongation and termination.

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  1. Department of Functional Genomics and Cancer, IGBMC, Illkirch Graffenstaden, France

    Carlos Mario Genes Robles & Frédéric Coin

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  1. Carlos Mario Genes Robles
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  2. Frédéric Coin
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Correspondence to Frédéric Coin.

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The authors declare no competing interests.

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Genes Robles, C.M., Coin, F. Conducting the CTD orchestra. Nat Chem Biol 15, 97–98 (2019). https://doi.org/10.1038/s41589-018-0201-6

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