Proteases influence colony aggregation behavior in Vibrio cholerae.
Proteases influence colony aggregation behavior in Vibrio cholerae.
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DOI：
10.1016/j.jbc.2023.105386
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发表时间：
2023-12
影响因子：
4.8
通讯作者：
Marletta, Michael A.
中科院分区：
文献类型：
--
作者：
Detomasi, Tyler C.;Batka, Allison E.;Valastyan, Julie S.;Hydorn, Molly A.;Craik, Charles S.;Bassler, Bonnie L.;Marletta, Michael A.
Aggregation behavior provides bacteria protection from harsh environments and threats to survival. Two uncharacterized proteases, LapX and Lap, are important for Vibrio cholerae liquid-based aggregation. Here, we determined that LapX is a serine protease with a preference for cleavage after glutamate and glutamine residues in the P1 position, which processes a physiologically based peptide substrate with a catalytic efficiency of 180 ± 80 M-1s-1. The activity with a LapX substrate identified by a multiplex substrate profiling by mass spectrometry screen was 590 ± 20 M-1s-1. Lap shares high sequence identity with an aminopeptidase (termed VpAP) from Vibrio proteolyticus and contains an inhibitory bacterial prepeptidase C-terminal domain that, when eliminated, increases catalytic efficiency on leucine p-nitroanilide nearly four-fold from 5.4 ± 4.1 × 104 M−1s−1 to 20.3 ± 4.3 × 104 M−1s−1. We demonstrate that LapX processes Lap to its mature form and thus amplifies Lap activity. The increase is approximately eighteen-fold for full-length Lap (95.7 ± 5.6 × 104 M−1s−1) and six-fold for Lap lacking the prepeptidase C-terminal domain (11.3 ± 1.9 × 105 M−1s−1). In addition, substrate profiling reveals preferences for these two proteases that could inform in vivo function. Furthermore, purified LapX and Lap restore the timing of the V. cholerae aggregation program to a mutant lacking the lapX and lap genes. Both proteases must be present to restore WT timing, and thus they appear to act sequentially: LapX acts on Lap, and Lap acts on the substrate involved in aggregation.
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影响因子：
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发表时间：
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影响因子：
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