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 accessAbstract
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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Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Cytoscape: A software Environment for integrated models of biomolecular interaction networks
Shannon, P., Markiel, A., Ozier, O., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., & Ideker, T. (2003) · Genome Research · doi:10.1101/gr.1239303 · Cited by 51,888
Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,355
Comparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977
Natural products as sources of new drugs over the last 25 years
Newman, D. J., & Cragg, G. M. (2007) · Journal of Natural Products · doi:10.1021/np068054v · Cited by 5,517
Natural products as sources of new drugs over the 30 years from 1981 to 2010
Newman, D. J., & Cragg, G. M. (2012) · Journal of Natural Products · doi:10.1021/np200906s · Cited by 4,687
The HHpred interactive server for protein homology detection and structure prediction
Soding, J., Biegert, A., & Lupas, A. N. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki408 · Cited by 3,740
Dali server: conservation mapping in 3D
Holm, L., & Rosenstr�m, P. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq366 · Cited by 3,640
Protein homology detection by HMM–HMM comparison
Söding, J. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti125 · Cited by 2,423
Arnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2013) · Nat. Prod. Rep. · doi:10.1039/c2np20085f · Cited by 2,076
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New developments in RiPP discovery, enzymology and engineering
Montalbán-López, M., Scott, T. A., Ramesh, S., Rahman, I. R., van Heel, A. J., Viel, J. H., Bandarian, V., Dittmann, E., Genilloud, O., Goto, Y., et al. (2021) · Natural Product Reports · doi:10.1039/d0np00027b · Cited by 787
Self-citationOrtega, M. A., & van der Donk, W. A. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2015.11.012 · Cited by 287
Biosynthesis and Chemical Applications of Thioamides
Mahanta, N., Szantai-Kis, D. M., Petersson, E. J., & Mitchell, D. A. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01022 · Cited by 218
Self-citationNguyen, D. T., Zhu, L., Gray, D. L., Woods, T. J., Padhi, C., Flatt, K. M., Mitchell, D. A., & van der Donk, W. A. (2024) · ACS Central Science · doi:10.1021/acscentsci.4c00088 · Cited by 51
Self-citationTranslation-Targeting RiPPs and Where to Find Them
Travin, D. Y., Bikmetov, D., & Severinov, K. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00226 · Cited by 19
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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