Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins.
Bacterial spores are protected by a coat consisting of about 60 different proteins assembled as a biochemically complex structure with intriguing morphological and mechanical properties. Historically, the coat has been considered a static structure providing rigidity and mainly acting as a sieve to...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2010-02-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2824812?pdf=render |
| _version_ | 1819264913497915392 |
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| author | Linda Ferencko Boris Rotman |
| author_facet | Linda Ferencko Boris Rotman |
| author_sort | Linda Ferencko |
| collection | DOAJ |
| description | Bacterial spores are protected by a coat consisting of about 60 different proteins assembled as a biochemically complex structure with intriguing morphological and mechanical properties. Historically, the coat has been considered a static structure providing rigidity and mainly acting as a sieve to exclude exogenous large toxic molecules, such as lytic enzymes. Over recent years, however, new information about the coat's architecture and function have emerged from experiments using innovative tools such as automated scanning microscopy, and high resolution atomic force microscopy.Using thin-section electron microscopy, we found that the coat of Bacillus spores has topologically specific proteins forming a layer that is identifiable because it spontaneously becomes decorated with hydrophobic fluorogenic probes from the milieu. Moreover, spores with decorated coat proteins (termed F-spores) have the unexpected attribute of responding to external germination signals by generating intense fluorescence. Fluorescence data from diverse experimental designs, including F-spores constructed from five different Bacilli species, indicated that the fluorogenic ability of F-spores is under control of a putative germination-dependent mechanism.This work uncovers a novel attribute of spore-coat proteins that we exploited to decorate a specific layer imparting germination-dependent fluorogenicity to F-spores. We expect that F-spores will provide a model system to gain new insights into structure/function dynamics of spore-coat proteins. |
| first_indexed | 2024-12-23T20:37:02Z |
| format | Article |
| id | doaj.art-566f51ccb0aa471f9e4c920a044fc03d |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-23T20:37:02Z |
| publishDate | 2010-02-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-566f51ccb0aa471f9e4c920a044fc03d2022-12-21T17:32:02ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-02-0152e928310.1371/journal.pone.0009283Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins.Linda FerenckoBoris RotmanBacterial spores are protected by a coat consisting of about 60 different proteins assembled as a biochemically complex structure with intriguing morphological and mechanical properties. Historically, the coat has been considered a static structure providing rigidity and mainly acting as a sieve to exclude exogenous large toxic molecules, such as lytic enzymes. Over recent years, however, new information about the coat's architecture and function have emerged from experiments using innovative tools such as automated scanning microscopy, and high resolution atomic force microscopy.Using thin-section electron microscopy, we found that the coat of Bacillus spores has topologically specific proteins forming a layer that is identifiable because it spontaneously becomes decorated with hydrophobic fluorogenic probes from the milieu. Moreover, spores with decorated coat proteins (termed F-spores) have the unexpected attribute of responding to external germination signals by generating intense fluorescence. Fluorescence data from diverse experimental designs, including F-spores constructed from five different Bacilli species, indicated that the fluorogenic ability of F-spores is under control of a putative germination-dependent mechanism.This work uncovers a novel attribute of spore-coat proteins that we exploited to decorate a specific layer imparting germination-dependent fluorogenicity to F-spores. We expect that F-spores will provide a model system to gain new insights into structure/function dynamics of spore-coat proteins.http://europepmc.org/articles/PMC2824812?pdf=render |
| spellingShingle | Linda Ferencko Boris Rotman Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins. PLoS ONE |
| title | Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins. |
| title_full | Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins. |
| title_fullStr | Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins. |
| title_full_unstemmed | Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins. |
| title_short | Constructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteins. |
| title_sort | constructing fluorogenic bacillus spores f spores via hydrophobic decoration of coat proteins |
| url | http://europepmc.org/articles/PMC2824812?pdf=render |
| work_keys_str_mv | AT lindaferencko constructingfluorogenicbacillussporesfsporesviahydrophobicdecorationofcoatproteins AT borisrotman constructingfluorogenicbacillussporesfsporesviahydrophobicdecorationofcoatproteins |