Crystal structure of the AlbEF complex involved in subtilosin A biosynthesis

Ishida, Kohki; Nakamura, Akira; Kojima, Shinichi

doi:10.1016/j.str.2022.10.002

Cited by 4 publications

(3 citation statements)

References 30 publications

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“…The proposed mechanism of action of bacilysin is that it interferes with bacterial cell wall synthesis by inhibiting glucosamine 6-phosphate (GlcN6P) synthase or fungal mannoprotein synthesis (Kenig et al 1976 ; Khan et al 2016 ). Subtilosin A is a 35-residue macrocyclic peptide encoded by the sbo-albABCDEFG gene cluster (Ishida et al 2022 ). The mature peptide is generated from its precursor by proteolytic cleavage of the N-terminal leader peptide and cyclization through covalent bonds between the N-terminal asparagine and the C-terminal glycine (Kawulka et al 2003 ).…”

Section: Discussionmentioning

confidence: 99%

Whole-genome sequencing and antimicrobial potential of bacteria isolated from Polish honey

Hafeez,

Pełka,

Buzun

et al. 2023

Appl Microbiol Biotechnol

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The aim of this study was the whole-genome analysis and assessment of the antimicrobial potential of bacterial isolates from honey harvested in one geographical location—the north of Poland. In total, 132 strains were derived from three honey samples, and the antimicrobial activity of CFAM (cell-free after-culture medium) was used as a criterion for strain selection and detailed genomic investigation. Two of the tested isolates (SZA14 and SZA16) were classified as Bacillus paralicheniformis, and one isolate (SZB3) as Bacillus subtilis based on their ANI and phylogenetic analysis relatedness. The isolates SZA14 and SZA16 were harvested from the same honey sample with a nucleotide identity of 98.96%. All three isolates have been found to be potential producers of different antimicrobial compounds. The secondary metabolite genome mining pipeline (antiSMASH) identified 14 gene cluster coding for non-ribosomal peptide synthetases (NRPs), polyketide synthases (PKSs), and ribosomally synthesized and post-translationally modified peptides (RiPPs) that are potential sources of novel antibacterials. The BAGEL4 analysis revealed the presence of nine putative gene clusters of interest in the isolates SZA14 and SZA16 (including the presence of six similar clusters present in both isolates, coding for the production of enterocin Nkr-5-3B, haloduracin-alpha, sonorensin, bottromycin, comX2, and lasso peptide), and four in B. subtilis isolate SZB3 (competence factor, sporulation-killing factor, subtilosin A, and sactipeptides). The outcomes of this study confirm that honey-derived Bacillus spp. strains can be considered potential producers of a broad spectrum of antimicrobial agents. Key points • Bacteria of the genus Bacillus are an important component of honey microbiota. • Honey-derived Bacillus spp. strains are potential producers of new antimicrobials.

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Section: Discussionmentioning

confidence: 99%

Whole-genome sequencing and antimicrobial potential of bacteria isolated from Polish honey

Hafeez,

Pełka,

Buzun

et al. 2023

Appl Microbiol Biotechnol

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“…In related M16A and M16C enzymes, these two subunits are combined in one ∼1,000 residue polypeptide; hence, these enzymes also have a pseudopeptidase domain that is critically important for the enzymatic function of the whole ( Li et al, 2006 ). Prokaryotic homologs of MPP have also been identified, produced from a two-gene operon reflecting the alpha/beta subunit arrangement seen in eukaryotic MPP ( Aleshin et al, 2009 ; Maruyama et al, 2011 ; Ishida et al, 2022 ). It is notable that the Core I and II proteins of the bc1 mitochondrial respiratory complex are homologous to alpha and beta MPP; in some cases these respiratory proteins are pseudopeptidases ( Braun and Schmitz, 1995 ; Taylor et al, 2001 ).…”

Section: Other Pseudometallopeptidasesmentioning

confidence: 99%

Inactive metallopeptidase homologs: the secret lives of pseudopeptidases

Lyons

2024

Front. Mol. Biosci.

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Inactive enzyme homologs, or pseudoenzymes, are proteins, found within most enzyme families, that are incapable of performing catalysis. Rather than catalysis, they are involved in protein-protein interactions, sometimes regulating the activity of their active enzyme cousins, or scaffolding protein complexes. Pseudoenzymes found within metallopeptidase families likewise perform these functions. Pseudoenzymes within the M14 carboxypeptidase family interact with collagens within the extracellular space, while pseudopeptidase members of the M12 “a disintegrin and metalloprotease” (ADAM) family either discard their pseudopeptidase domains as unnecessary for their roles in sperm maturation or utilize surface loops to enable assembly of key complexes at neuronal synapses. Other metallopeptidase families contain pseudopeptidases involved in protein synthesis at the ribosome and protein import into organelles, sometimes using their pseudo-active sites for these interactions. Although the functions of these pseudopeptidases have been challenging to study, ongoing work is teasing out the secret lives of these proteins.

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“…24 The thioether bonds are installed in the precursor peptide SboA by the radical SAM enzyme AlbA 25 and heterologous generation of the thioether linkages in Escherichia coli has been achieved. 26 However, the head-to-tail cyclisation, proposed to be catalysed by a protease encoded in the subtilosin biosynthetic gene cluster, 27,28 has not been reconstituted. Thus, we sought to achieve this final maturation step by OaAEP1-mediated cyclisation (Fig.…”

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confidence: 99%