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A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils

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Claessen, Dennis, Rink, Rick, de Jong, Wouter, Siebring, Jeroen, de Vreugd, Peter, Boersma, F.G. Hidde, Dijkhuizen, Lubbert, Wösten, Han A.B.·2003·Genes & Development
DOI 10.1101/gad.264303PMC PMC196180
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Abstract

Streptomycetes exhibit a complex morphological differentiation. After a submerged mycelium has been formed, filaments grow into the air to septate into spores. A class of eight hydrophobic secreted proteins, ChpA–H, was shown to be instrumental in the development of Streptomyces coelicolor . Mature forms of ChpD–H are up to 63 amino acids in length, and those of ChpA–C are larger (±225 amino acids). ChpA–C contain two domains similar to ChpD–H, as well as a cell-wall sorting signal. The chp genes were expressed in submerged mycelium ( chpE and chpH ) as well as in aerial hyphae ( chpA–H ). Formation of aerial hyphae was strongly affected in a strain in which six chp genes were deleted (Δ chpABCDEH ). A mixture of ChpD–H purified from cell walls of aerial hyphae complemented the Δ chpABCDEH strain extracellularly, and it accelerated development in the wild-type strain. The protein mixture was highly surface active, and it self-assembled into amyloid-like fibrils at the water–air interface. The fibrils resembled those of a surface layer of aerial hyphae. We thus conclude that the amyloid-like fibrils of ChpD–H lower the water surface tension to allow aerial growth and cover aerial structures, rendering them hydrophobic. ChpA–C possibly bind ChpD–H to the cell wall.

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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 [66]

    The Identification and characterization section and Figure 2 caption describe secretion signal sequences and hydrophobic regions in all eight chaplins. They do not give a length of about 40 residues for a chaplin domain; they also describe two chaplin-like regions in the larger ChpA–C proteins, rather than one. Page numbers are unavailable in our copy. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Chaplins A-C are anchored to the peptidoglycan via sorting signals with a LAXTG motif, allowing the smaller chaplins D-H to be immobilized and nucleated on the cell surface by interaction with their chaplin domains.

    “It is suggested that chaplins A -C are anchored to the peptidoglycan via sorting signals with a LAXTG motif, allowing the smaller chaplins DH to be immobilized and nucleated on the cell surface by interaction with their chaplin domains (Fig. 7) [66].”

    From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [66]

    The Discussion (page unavailable) proposes that ChpA-C may be linked to peptidoglycan through their LAXTG motifs and coassemble with ChpD-H through homologous sequences, thereby immobilizing the smaller chaplins at the cell surface. It does not say that ChpA-C nucleate ChpD-H assembly; that additional mechanism is unsupported. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • 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 [66]

    The ‘Identification and characterization of the chaplins of S. coelicolor’ section (page not provided) says the authors identified eight homologous genes and named them chaplins, not six. The ‘Chaplins are involved in formation of aerial hyphae’ section supports their role in aerial hyphae formation; it describes deletion of up to six genes, which does not make the identified set six genes. (LLM, conf=0.90)

    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 [66]

  • 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 [66]

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Authors
Claessen, D., Rink, R., de Jong, W., Siebring, J., de Vreugd, P., Boersma, F. G. H., Dijkhuizen, L., & Wösten, H. A. B.
Affiliations
  • University of Groningen (NL)
  • Utrecht University (NL)
ORCID
Venue
Genes & Development
Publisher
Cold Spring Harbor Laboratory
Published
2003-06-27
Volume
17
Issue
14
Pages
1714-1726
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
DOI
10.1101/gad.264303
PMC
PMC196180
OpenAlex
W2129115026
Cited by
327
References
41
Citations by year
2026: 6 · 2025: 4 · 2024: 7 · 2023: 10 · 2022: 10 · 2021: 13 · 2020: 14 · 2019: 14 · 2018: 15 · 2017: 20 · 2016: 13 · 2015: 14 · 2014: 19 · 2013: 18 · 2012: 26
Type
posted content
Language
en
Open access
Locations
  • Genes & Development (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
  • Leiden Repository (Leiden University) (submittedVersion)
  • Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
  • University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
Topics
  • Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
Streptomyces coelicolor, aerial hyphae formation, amyloid-like fibrils, water surface tension, morphological differentiation
MeSH terms
Amino Acid Sequence, Molecular Sequence Data, Proteins, Streptomyces, Hyphae, Hydrophobic and Hydrophilic Interactions

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