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<p>Bacteria produce a variety of peptides to mediate nutrient acquisition, microbial interactions and other physiological processes. Of special interest are surface-active peptides that aid in growth and development. Herein we report the structure and characterization of clavusporins, unusual and hydrophobic ribosomal peptides with multiple C-methylations at unactivated carbon centers, which help drastically reduce the surface tension of water and thereby aid in <i>Streptomyces</i> development. The peptides are synthesized by a previously uncharacterized protein superfamily, termed DUF5825, in conjunction with a vitamin B<sub>12</sub>-dependent radical <i>S</i>-adenosylmethionine metalloenzyme. The operon encoding clavusporins is widespread among actinomycete bacteria, suggesting a prevalent role for clavusporins as morphogens in erecting aerial hyphae and thereby advancing sporulation and proliferation.</p><p></p>

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Peptide surfactants with post-translational C-methylations that promote bacterial development

  • 期刊论文

  • 发表日期：

    2025年4月22日

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  • Chen Zhang,
  • Yuchen Li,
  • Ellysia N. Overton,
  • Mohammad R. Seyedsayamdost

摘要

Bacteria produce a variety of peptides to mediate nutrient acquisition, microbial interactions and other physiological processes. Of special interest are surface-active peptides that aid in growth and development. Herein we report the structure and characterization of clavusporins, unusual and hydrophobic ribosomal peptides with multiple C-methylations at unactivated carbon centers, which help drastically reduce the surface tension of water and thereby aid in Streptomyces development. The peptides are synthesized by a previously uncharacterized protein superfamily, termed DUF5825, in conjunction with a vitamin B12-dependent radical S-adenosylmethionine metalloenzyme. The operon encoding clavusporins is widespread among actinomycete bacteria, suggesting a prevalent role for clavusporins as morphogens in erecting aerial hyphae and thereby advancing sporulation and proliferation.