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The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.

A prevalent peptide-binding domain guides ribosomal natural product biosynthesis

Open access
Burkhart, Brandon J, Hudson, Graham A, Dunbar, Kyle L, Mitchell, Douglas A·2015·Nature Chemical Biology

Abstract

Ribosomally synthesized and posttranslationally modified peptides (RiPPs) are a rapidly growing natural product class. RiPP precursor peptides can undergo extensive enzymatic tailoring, yielding structurally and functionally diverse products, and their biosynthetic logic makes them attractive bioengineering targets. Recent work suggests that unrelated RiPP modifying enzymes contain structurally similar precursor peptide-binding domains. Using profile hidden Markov model comparisons, we discovered related and previously unrecognized peptide-binding domains in proteins spanning the majority of known prokaryotic RiPP classes; thus, we named this conserved domain the RiPP precursor peptide recognition element (RRE). Through binding studies, we verify the role of the RRE for three distinct RiPP classes: linear azole-containing peptides, thiopeptides, and lasso peptides. Because numerous RiPP biosynthetic enzymes act on peptide substrates, our findings have powerful predictive value as to which protein(s) drive substrate binding, laying a foundation for further characterization of RiPP biosynthetic pathways and the rational engineering of new peptide-binding activities.

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Metadata

Authors
Burkhart, B. J., Hudson, G. A., Dunbar, K. L., & Mitchell, D. A.
Venue
Nature Chemical Biology
Published
2015-07-13
Volume
11
Issue
8
Pages
564-570
ISSN
  • 1552-4450 (ISSN-L)
  • 1552-4469
OpenAlex
W1587997563
Cited by
374
References
51
FWCI
22.42
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: A prevalent peptide-binding domain guides ribosomal natural product biosynthesis. https://app.cochat.ai/papers/10.1038/nchembio.1856
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Burkhart, B. J., Hudson, G. A., Dunbar, K. L., & Mitchell, D. A. (2015). A prevalent peptide-binding domain guides ribosomal natural product biosynthesis. Nature Chemical Biology. https://doi.org/10.1038/nchembio.1856

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.