The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor

Elliot, Marie A.; Karoonuthaisiri, Nitsara; Huang, Jianqiang; Bibb, Maureen J.; Cohen, Stanley N.; Kao, Camilla M.; Buttner, Mark J.

doi:10.1101/gad.264403

Cited by 246Bacterial Genetics and BiotechnologyMicrobial Natural Products and BiosynthesisBiochemical and Structural Characterization

The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor

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Elliot, Marie A., Karoonuthaisiri, Nitsara, Huang, Jianqiang, Bibb, Maureen J., Cohen, Stanley N., Kao, Camilla M., Buttner, Mark J.·2003·Genes & Development

DOI 10.1101/gad.264403PMC PMC196181

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Abstract

The filamentous bacterium Streptomyces coelicolor differentiates by forming specialized, spore-bearing aerial hyphae that grow into the air. Using microarrays, we identified genes that are down-regulated in a mutant unable to erect aerial hyphae. Through this route, we identified a previously unknown layer of aerial mycelium surface proteins (the “chaplins”). The chaplins share a hydrophobic domain of ∼40 residues (the “chaplin domain”), and all have a secretion signal. The five short chaplins (ChpD,E,F,G,H) have one chaplin domain, whereas the three long chaplins (ChpA,B,C) have two chaplin domains and a C-terminal “sorting signal” that targets them for covalent attachment to the cell wall by sortase enzyme. Expression of the two chaplin genes examined ( chpE, chpH ) depended on aerial hyphae formation but not sporulation, and egfp fusions showed their expression localized to aerial structures. Mass spectrometry of cell wall extracts confirmed that the short chaplins localized to the cell surface. Deletion of chaplin genes caused severe delays in aerial hyphae formation, a phenotype rescued by exogenous application of chaplin proteins. These observations implicate the chaplins in aerial mycelium formation, and suggest that coating of the envelope by the chaplins is required for aerial hyphae to grow out of the aqueous environment of the substrate mycelium into the air.

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Two groups identified a set of six genes encoding proteins likely involved in aerial hyphae formation, named chaplins.
“Recently, two groups have identified a set of six genes encoding proteins that are likely involved in aerial hyphae formation and which were named chaplins [66,67].”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [67]
The Identification section names the chaplin genes chpA–H, and the A model of chaplin assembly and function section explicitly says the family has eight members, not six. The paper does support their involvement in aerial mycelium formation and refers to an accompanying manuscript by another group. (LLM, conf=0.89)
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All chaplins are synthesized as precursors with an N-terminal leader sequence and a short hydrophobic domain (chaplin domain) of about 40 residues.
“All chaplins are synthesized as precursors with an N-terminal leader sequence and a short hydrophobic domain (chaplin domain) of about 40 residues.”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [67]
The Identification section (page unavailable) describes a very hydrophobic chaplin domain shared by the family and refers to cleavage of a leader peptide in the long chaplins. The SapB section (page unavailable) also refers to signal peptides in the eight chaplins. The body passages do not establish the claimed domain length of about 40 residues. (LLM, conf=0.83)
Experimental — accuracy not yet measured
Deletion of six chaplin genes (chpA-H) hindered the formation of aerial hyphae; the defect could be complemented by the addition of exogenous chaplin proteins.
“Deletion of six chaplin genes (chpA -H) hindered the formation of aerial hyphae; the defect could be complemented by the addition of exogenous chaplin proteins.”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [67]
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Experimental — accuracy not yet measured
Chaplins D-H are very short polypeptides, whereas chaplins A-C are longer and carry a C-terminal sorting signal (LAXTG motif).
“Chaplins D -H are very short polypeptides, whereas chaplins A -C are longer and carry a C-terminal sorting signal (LAXTG motif).”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [67]

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Capstick, D. S., Willey, J. M., Buttner, M. J., & Elliot, M. A. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05674.x · Cited by 76 · see citing works
Self-citation
Aerial development in Streptomyces coelicolor requires sortase activity
Duong, A., Capstick, D. S., Berardo, C. D., Findlay, K., Hesketh, A. R., Hong, H., & Elliot, M. A. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.07983.x · Cited by 42 · see citing works
Self-citation

Authors: Elliot, M. A., Karoonuthaisiri, N., Huang, J., Bibb, M. J., Cohen, S. N., Kao, C. M., & Buttner, M. J.
Affiliations: John Innes Centre (GB)
Stanford University (US)
Stanford Medicine (US)
ORCID: Elliot, Marie A.
Karoonuthaisiri, Nitsara
Huang, Jianqiang
Bibb, Maureen J.
Cohen, Stanley N.
Kao, Camilla M.
Buttner, Mark J.
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2003-06-27
Volume: 17
Issue: 14
Pages: 1727-1740
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.264403
PMC: PMC196181
OpenAlex: W2126316619
Cited by: 246
References: 62
Citations by year: 2026: 6 · 2025: 4 · 2024: 3 · 2023: 4 · 2022: 7 · 2021: 21 · 2020: 10 · 2019: 12 · 2018: 10 · 2017: 18 · 2016: 7 · 2015: 7 · 2014: 14 · 2013: 10 · 2012: 23
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Fondation pour la Recherche Médicale
Biotechnology and Biological Sciences Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords: Charlie Chaplin, Streptomyces coelicolor, aerial hyphae formation, aerial mycelium, cell surface proteins, hydrophobic domains, sortase, gene expression regulation
MeSH terms: Amino Acid Sequence, Cell Wall, Molecular Sequence Data, Proteins, Streptomyces, Sequence Alignment, Gene Expression Profiling, Hyphae, Hydrophobic and Hydrophilic Interactions

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The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor

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