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Poles Apart: Where and How Cells Construct Nisin

Nisin is a 34-amino-acid lantibiotic that has been used commercially for almost a century as a food preservative. In order to produce active nisin, Lactococcus lactis requires an 11-gene operon that encodes proteins involved in modification, processing, transport, immunity, and regulation. While the...

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Autor principal: Hill, Colin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773994/
https://www.ncbi.nlm.nih.gov/pubmed/33323521
http://dx.doi.org/10.1128/mBio.02991-20
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author Hill, Colin
author_facet Hill, Colin
author_sort Hill, Colin
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description Nisin is a 34-amino-acid lantibiotic that has been used commercially for almost a century as a food preservative. In order to produce active nisin, Lactococcus lactis requires an 11-gene operon that encodes proteins involved in modification, processing, transport, immunity, and regulation. While the role of each of the 11 proteins is well understood, the location and spatial organization of the biosynthetic machinery that involves NisA, NisB, NisC, NisT, and NisP remain to be determined. In this elegant paper (J. Chen, A. J. van Heel, and O. P. Kuipers, mBio 11:e02825-20, 2020, https://doi.org/10.1128/mBio.02825-20), we learn that a NisB dimer is recruited to the “old” pole of a dividing cell, where it assembles with NisC to form a modification complex that can engage with NisA. Unexpectedly, the NisT transporter does not stably assemble into this complex but is distributed around the membrane until it engages with the NisABC complex to transport NisA across the membrane, whereupon it dissociates from NisBC.
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spelling pubmed-77739942021-01-05 Poles Apart: Where and How Cells Construct Nisin Hill, Colin mBio Commentary Nisin is a 34-amino-acid lantibiotic that has been used commercially for almost a century as a food preservative. In order to produce active nisin, Lactococcus lactis requires an 11-gene operon that encodes proteins involved in modification, processing, transport, immunity, and regulation. While the role of each of the 11 proteins is well understood, the location and spatial organization of the biosynthetic machinery that involves NisA, NisB, NisC, NisT, and NisP remain to be determined. In this elegant paper (J. Chen, A. J. van Heel, and O. P. Kuipers, mBio 11:e02825-20, 2020, https://doi.org/10.1128/mBio.02825-20), we learn that a NisB dimer is recruited to the “old” pole of a dividing cell, where it assembles with NisC to form a modification complex that can engage with NisA. Unexpectedly, the NisT transporter does not stably assemble into this complex but is distributed around the membrane until it engages with the NisABC complex to transport NisA across the membrane, whereupon it dissociates from NisBC. American Society for Microbiology 2020-12-15 /pmc/articles/PMC7773994/ /pubmed/33323521 http://dx.doi.org/10.1128/mBio.02991-20 Text en Copyright © 2020 Hill. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Commentary
Hill, Colin
Poles Apart: Where and How Cells Construct Nisin
title Poles Apart: Where and How Cells Construct Nisin
title_full Poles Apart: Where and How Cells Construct Nisin
title_fullStr Poles Apart: Where and How Cells Construct Nisin
title_full_unstemmed Poles Apart: Where and How Cells Construct Nisin
title_short Poles Apart: Where and How Cells Construct Nisin
title_sort poles apart: where and how cells construct nisin
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773994/
https://www.ncbi.nlm.nih.gov/pubmed/33323521
http://dx.doi.org/10.1128/mBio.02991-20
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