Faced with nutritional stress, some bacteria form endospores that can survive extreme conditions for long periods of time; yet the function of many proteins expressed during sporulation remains a mystery. We show that one such protein, KapD, is a 3 prime exoribonuclease expressed under control of the mother cell-specific transcription factors SigE and SigK in B. subtilis. KapD assembles dynamically over the spore surface through a direct interaction with the major crust protein CotY. KapD catalytic activity is required for the normal adhesiveness of spore surface layers. We identify the sigK mRNA as a key substrate for KapD and show that its sequestration by CotY controls the stability of the sigK transcript. SigK is controlled through excision of a prophage-like element, transcriptional regulation, and removal of an inhibitory pro-sequence. We reveal a fourth, posttranscriptional layer of control of sigK expression that couples late-stage gene expression in the mother cell to spore morphogenesis.
[doi:10.25345/C5KH0FB19]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Post-transcriptional regulation ; Cell development ; Sporulation ; RNA degradation ; Q-Exactive plus ; Maxquant ; DatasetType:Proteomics
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Alexandre D'Halluin, Institut de Biologie Physico-Chimique, FRANCE |
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