Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins
Most bacteria are in fierce competition with other species for limited nutrients. Some bacteria can kill nearby cells by secreting bacteriocins, a diverse group of proteinaceous antimicrobials. However, bacteriocins are typically freely diffusible, and so of little value to planktonic cells in aqueo...
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Format: | Article |
Language: | en_US |
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eLife Sciences Publications, Ltd.
2017
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Online Access: | http://hdl.handle.net/1721.1/109871 https://orcid.org/0000-0002-6720-2323 https://orcid.org/0000-0002-8288-7607 |
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author | Garcia Bayona, Leonor Guo, Monica S Laub, Michael T |
author2 | Massachusetts Institute of Technology. Department of Biology |
author_facet | Massachusetts Institute of Technology. Department of Biology Garcia Bayona, Leonor Guo, Monica S Laub, Michael T |
author_sort | Garcia Bayona, Leonor |
collection | MIT |
description | Most bacteria are in fierce competition with other species for limited nutrients. Some bacteria can kill nearby cells by secreting bacteriocins, a diverse group of proteinaceous antimicrobials. However, bacteriocins are typically freely diffusible, and so of little value to planktonic cells in aqueous environments. Here, we identify an atypical two-protein bacteriocin in the α-proteobacterium Caulobacter crescentus that is retained on the surface of producer cells where it mediates cell contact-dependent killing. The bacteriocin-like proteins CdzC and CdzD harbor glycine-zipper motifs, often found in amyloids, and CdzC forms large, insoluble aggregates on the surface of producer cells. These aggregates can drive contact-dependent killing of other organisms, or Caulobacter cells not producing the CdzI immunity protein. The Cdz system uses a type I secretion system and is unrelated to previously described contact-dependent inhibition systems. However, Cdz-like systems are found in many bacteria, suggesting that this form of contact-dependent inhibition is common. |
first_indexed | 2024-09-23T12:51:41Z |
format | Article |
id | mit-1721.1/109871 |
institution | Massachusetts Institute of Technology |
language | en_US |
last_indexed | 2024-09-23T12:51:41Z |
publishDate | 2017 |
publisher | eLife Sciences Publications, Ltd. |
record_format | dspace |
spelling | mit-1721.1/1098712022-09-28T10:34:55Z Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins Garcia Bayona, Leonor Guo, Monica S Laub, Michael T Massachusetts Institute of Technology. Department of Biology Garcia Bayona, Leonor Guo, Monica S Laub, Michael T Most bacteria are in fierce competition with other species for limited nutrients. Some bacteria can kill nearby cells by secreting bacteriocins, a diverse group of proteinaceous antimicrobials. However, bacteriocins are typically freely diffusible, and so of little value to planktonic cells in aqueous environments. Here, we identify an atypical two-protein bacteriocin in the α-proteobacterium Caulobacter crescentus that is retained on the surface of producer cells where it mediates cell contact-dependent killing. The bacteriocin-like proteins CdzC and CdzD harbor glycine-zipper motifs, often found in amyloids, and CdzC forms large, insoluble aggregates on the surface of producer cells. These aggregates can drive contact-dependent killing of other organisms, or Caulobacter cells not producing the CdzI immunity protein. The Cdz system uses a type I secretion system and is unrelated to previously described contact-dependent inhibition systems. However, Cdz-like systems are found in many bacteria, suggesting that this form of contact-dependent inhibition is common. United States. National Institutes of Health (R01GM082899) 2017-06-14T20:07:47Z 2017-06-14T20:07:47Z 2017-03 2017-01 Article http://purl.org/eprint/type/JournalArticle 2050-084X http://hdl.handle.net/1721.1/109871 García-Bayona, Leonor; Guo, Monica S and Laub, Michael T. “Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins.” eLife 6 (March 2017): e24869 © 2017, García-Bayona et al https://orcid.org/0000-0002-6720-2323 https://orcid.org/0000-0002-8288-7607 en_US http://dx.doi.org/10.7554/eLife.24869 eLife Creative Commons Attribution 4.0 International License http://creativecommons.org/licenses/by/4.0/ application/pdf eLife Sciences Publications, Ltd. eLife |
spellingShingle | Garcia Bayona, Leonor Guo, Monica S Laub, Michael T Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins |
title | Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins |
title_full | Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins |
title_fullStr | Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins |
title_full_unstemmed | Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins |
title_short | Contact-Dependent Killing by Caulobacter Crescentus via Cell Surface-Associated, Glycine Zipper Proteins |
title_sort | contact dependent killing by caulobacter crescentus via cell surface associated glycine zipper proteins |
url | http://hdl.handle.net/1721.1/109871 https://orcid.org/0000-0002-6720-2323 https://orcid.org/0000-0002-8288-7607 |
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