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Dormant spores sense amino acids through the B subunits of their germination receptors

Author

Listed:
  • Lior Artzi

    (Harvard Medical School)

  • Assaf Alon

    (Harvard Medical School)

  • Kelly P. Brock

    (Harvard Medical School)

  • Anna G. Green

    (Harvard Medical School)

  • Amy Tam

    (Harvard Medical School)

  • Fernando H. Ramírez-Guadiana

    (Harvard Medical School)

  • Debora Marks

    (Harvard Medical School)

  • Andrew Kruse

    (Harvard Medical School)

  • David Z. Rudner

    (Harvard Medical School)

Abstract

Bacteria from the orders Bacillales and Clostridiales differentiate into stress-resistant spores that can remain dormant for years, yet rapidly germinate upon nutrient sensing. How spores monitor nutrients is poorly understood but in most cases requires putative membrane receptors. The prototypical receptor from Bacillus subtilis consists of three proteins (GerAA, GerAB, GerAC) required for germination in response to L-alanine. GerAB belongs to the Amino Acid-Polyamine-Organocation superfamily of transporters. Using evolutionary co-variation analysis, we provide evidence that GerAB adopts a structure similar to an L-alanine transporter from this superfamily. We show that mutations in gerAB predicted to disrupt the ligand-binding pocket impair germination, while mutations predicted to function in L-alanine recognition enable spores to respond to L-leucine or L-serine. Finally, substitutions of bulkier residues at these positions cause constitutive germination. These data suggest that GerAB is the L-alanine sensor and that B subunits in this broadly conserved family function in nutrient detection.

Suggested Citation

  • Lior Artzi & Assaf Alon & Kelly P. Brock & Anna G. Green & Amy Tam & Fernando H. Ramírez-Guadiana & Debora Marks & Andrew Kruse & David Z. Rudner, 2021. "Dormant spores sense amino acids through the B subunits of their germination receptors," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27235-2
    DOI: 10.1038/s41467-021-27235-2
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    References listed on IDEAS

    as
    1. Renhong Yan & Xin Zhao & Jianlin Lei & Qiang Zhou, 2019. "Structure of the human LAT1–4F2hc heteromeric amino acid transporter complex," Nature, Nature, vol. 568(7750), pages 127-130, April.
    2. Anna G. Green & Hadeer Elhabashy & Kelly P. Brock & Rohan Maddamsetti & Oliver Kohlbacher & Debora S. Marks, 2021. "Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    3. Manuele Rebsamen & Lorena Pochini & Taras Stasyk & Mariana E. G. de Araújo & Michele Galluccio & Richard K. Kandasamy & Berend Snijder & Astrid Fauster & Elena L. Rudashevskaya & Manuela Bruckner & St, 2015. "SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1," Nature, Nature, vol. 519(7544), pages 477-481, March.
    4. Katharina E. J. Jungnickel & Joanne L. Parker & Simon Newstead, 2018. "Structural basis for amino acid transport by the CAT family of SLC7 transporters," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
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    Cited by:

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    2. Takeaki Tezuka & Kyota Mitsuyama & Risa Date & Yasuo Ohnishi, 2023. "A unique sigma/anti-sigma system in the actinomycete Actinoplanes missouriensis," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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