Methanobactins: Structures, Biosynthesis, and Microbial Diversity

Reyvin M. Reyes, Amy C. Rosenzweig

Research output: Contribution to journalReview articlepeer-review

5 Scopus citations

Abstract

Methanobactins (Mbns) are ribosomally synthesized and posttranslationally modified peptide natural products released by methanotrophic bacteria under conditions of copper scarcity. Mbns bind Cu(I) with high affinity via nitrogen-containing heterocycles and thioamide groups installed on a precursor peptide, MbnA, by a core biosynthetic enzyme complex, MbnBC. Additional stabilizing modifications are enacted by other, less universal biosynthetic enzymes. Copper-loaded Mbn is imported into the cell by TonB-dependent transporters called MbnTs, and copper is mobilized by an unknown mechanism. The machinery to biosynthesize and transport Mbn is encoded in operons that are also found in the genomes of nonmethanotrophic bacteria. In this review, we provide an update on the state of the Mbn field, highlighting recent discoveries regarding Mbn structure, biosynthesis, and handling as well as the emerging roles of Mbns in the environment and their potential use as therapeutics.

Original languageEnglish (US)
Pages (from-to)383-401
Number of pages19
JournalAnnual Review of Microbiology
Volume78
Issue number1
DOIs
StatePublished - Aug 9 2024

Funding

Work in the Rosenzweig lab on methanobactins is supported by National Institutes of Health grant GM118035 (to A.C.R.).

Keywords

  • RiPP natural product
  • chalkophore
  • copper homeostasis
  • methanobactin
  • methanotroph

ASJC Scopus subject areas

  • Microbiology

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