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Yasuo Ohnishi

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Open access Sep 2026

Components of the Clp complex are required for sporangium formation and dehiscence in Actinoplanes missouriensis

ABSTRACT The actinomycete Actinoplanes missouriensis forms terminal sporangia that contain a few hundred spores. When immersed in water, the sporangium opens to release spores, which start swimming using flagella, via a process referred to as sporangium dehiscence. In this study, we conducted a functional analysis of genes encoding the components of the caseinolytic protease (Clp) complex, which comprises ATPase (chaperone) subunits (ClpX and ClpC) and proteolytic subunits (ClpP1–4). The clpX null mutant (ΔclpX) strain formed sporangia smaller than the wild-type strain. The small sporangia scarcely opened under conditions that induce sporangium dehiscence in the wild-type strain. Consistently, the number of released spores was three orders of magnitude lower in the ΔclpX strain than in the wild-type strain. S1 nuclease mapping determined two transcriptional start points of clpX (TSSU and TSSD for upstream and downstream, respectively). A housekeeping sigma factor-dependent promoter and a FliA-family sigma factor-dependent promoter were found upstream of TSSU and TSSD, respectively. A gene complementation test showed that apparently normal sporangium formation in the ΔclpX strain was restored by the introduction of clpX with either of the two promoters, whereas both promoters were required for sporangium dehiscence. Meanwhile, mutant strains that produced ClpC with T30S or I33F/L34F replacements, which presumably reduced their substrate-binding activity, produced sporangia with irregular shapes. Furthermore, gene disruption experiments of four putative proteolytic subunit genes indicated that clpP3 is conditionally involved in sporangium dehiscence. We concluded that sporangium formation and dehiscence are regulated at the post-translational level via proteolysis by Clp complexes in A. missouriensis. IMPORTANCE Actinoplanes missouriensis has a complex life cycle, in which the sporangium containing a few hundred flagellated spores is the most characteristic structure. Spores are released from sporangia via a process called sporangium dehiscence. We have revealed that sporangium formation and dehiscence are regulated by several transcriptional regulators; however, post-transcriptional regulation of sporangium formation and dehiscence remains unknown. In the present study, we revealed that two ATPase components of the Clp complex, ClpC and ClpX, and a proteolytic component, ClpP3, are involved in sporangium formation and/or dehiscence. This study indicates that in addition to transcriptional regulation, proteolysis regulated by Clp complexes is another crucial factor in the morphological development of A. missouriensis. Actinoplanes missouriensis has a complex life cycle, in which the sporangium containing a few hundred flagellated spores is the most characteristic structure. Spores are released from sporangia via a process called sporangium dehiscence. We have revealed that sporangium formation and dehiscence are regulated by several transcriptional regulators; however, post-transcriptional regulation of sporangium formation and dehiscence remains unknown. In the present study, we revealed that two ATPase components of the Clp complex, ClpC and ClpX, and a proteolytic component, ClpP3, are involved in sporangium formation and/or dehiscence. This study indicates that in addition to transcriptional regulation, proteolysis regulated by Clp complexes is another crucial factor in the morphological development of A. missouriensis.

Ryota Suzuki, Manato Maruko, Remi Suzuki et al. · 0 citations
Open access Jul 2026

Mechanism for Aromatic Nitration Catalyzed by Cytochrome P450 Enzymes from Rufomycin Biosynthesis

During the biosynthesis of the peptide antibiotic rufomycin, the cytochrome P450 (P450) enzyme RufO catalyzes the aromatic nitration of a tyrosine residue in a ribosomal pentapeptide that serves as a precursor for nonribosomal peptide synthesis. To understand the mechanism of this unusual P450-mediated reaction, a series of pentapeptides were tested as substrates alongside molecular dynamics simulations and quantum mechanics/molecular mechanics (QM/MM, ONIOM approach) calculations. A new substrate-bound crystal structure of the homologue NsRufO was also obtained. These experiments revealed the intimate and necessary involvement of a histidine residue within the pentapeptide substrate of RufO in supporting effective nitration, with the protonation state of the intermediate compound II proposed to influence the production of nitrated tyrosine over unwanted nitrate formation. These findings provide key insights into the mechanism of P450-mediated nitration that explain how sequence differences in RufO and its homologues, along with the structure of the pentapeptide substrate, facilitate aromatic nitration of tyrosine by RufO.

A. M. Kirk, Jemma Gullick, Yong-Wei Zhao et al. · 0 citations
Open access Aug 2026

Promiscuous ATP-Dependent Diazotases Discovered by Comprehensive Genome Mining Based on Sequence Similarity Network Analysis

This systematic analysis of ATP-dependent diazotases from actinomycetes that catalyze the condensation of nitrite with aromatic amines establishes group 3 diazotases as promising, engineerable biocatalysts for selective and efficient diazo installation.

Jia-Yu Ning, Seiji Kawai, Y. Katsuyama et al. · 0 citations

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