The ATP-dependent protease ClpYQ degrades cell division proteins DivIVA and Mbl inBacillus subtilis

2024 · doi:10.1101/2024.10.15.618472
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The study examined which protein substrates are targeted by the ATP-dependent protease ClpYQ in Bacillus subtilis, focusing on two divisome/elongasome-associated proteins predicted by prior quantitative proteomics. Using both in vitro and in vivo experiments, the authors confirmed that ClpYQ degrades DivIVA and Mbl, thereby identifying the first characterized ClpYQ substrates and supporting a role in regulating cell division and elongation. The paper notes that previous genetic data showed clpQ is synthetically lethal with clpP while each gene alone is non-essential, implying possible redundancy with ClpXP, which is relevant to interpreting broader regulatory roles. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Abstract

ATP-dependent proteases play key roles in bacterial protein quality control and regulation of cellular processes. ClpYQ and ClpXP are ATP-dependent proteases in the Gram-positive bacteria Bacillus subtilis . To date, no substrate proteins of B. subtilis ClpYQ have been characterized. The protease component encoded by clpQ is synthetically lethal with clpP and the two genes are non-essential individually, suggesting potentially redundant roles for ClpYQ and ClpXP. Previous quantitative proteomic data predicted that B. subtilis proteins DivIVA and Mbl, components of the divisome and elongasome respectively, are potential substrates of ClpYQ. The role of DivIVA and Mbl in cell division and elongation suggests a significant role of ClpYQ in regulating cell division through targeted degradation of key divisome and elongasome proteins. Here we confirm that DivIVA and Mbl are degraded by ClpYQ both in vitro and in vivo , and thus identify the first two substrates of ClpYQ in B. subtilis .
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Abstract ATP-dependent proteases play key roles in bacterial protein quality control and regulation of cellular processes. ClpYQ and ClpXP are ATP-dependent proteases in the Gram-positive bacteria Bacillus subtilis. To date, no substrate proteins of B. subtilis ClpYQ have been characterized. The protease component encoded by clpQ is synthetically lethal with clpP and the two genes are non-essential individually, suggesting potentially redundant roles for ClpYQ and ClpXP. Previous quantitative proteomic data predicted that B. subtilis proteins DivIVA and Mbl, components of the divisome and elongasome respectively, are potential substrates of ClpYQ. The role of DivIVA and Mbl in cell division and elongation suggests a significant role of ClpYQ in regulating cell division through targeted degradation of key divisome and elongasome proteins. Here we confirm that DivIVA and Mbl are degraded by ClpYQ both in vitro and in vivo, and thus identify the first two substrates of ClpYQ in B. subtilis. Competing Interest Statement The authors have declared no competing interest.

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