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Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast.

Publication ,  Journal Article
Johnson, CR; Steingesser, MG; Weems, AD; Khan, A; Gladfelter, A; Bertin, A; McMurray, MA
Published in: Elife
January 28, 2020

Septin proteins evolved from ancestral GTPases and co-assemble into hetero-oligomers and cytoskeletal filaments. In Saccharomyces cerevisiae, five septins comprise two species of hetero-octamers, Cdc11/Shs1-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11/Shs1. Slow GTPase activity by Cdc12 directs the choice of incorporation of Cdc11 vs Shs1, but many septins, including Cdc3, lack GTPase activity. We serendipitously discovered that guanidine hydrochloride rescues septin function in cdc10 mutants by promoting assembly of non-native Cdc11/Shs1-Cdc12-Cdc3-Cdc3-Cdc12-Cdc11/Shs1 hexamers. We provide evidence that in S. cerevisiae Cdc3 guanidinium occupies the site of a 'missing' Arg side chain found in other fungal species where (i) the Cdc3 subunit is an active GTPase and (ii) Cdc10-less hexamers natively co-exist with octamers. We propose that guanidinium reactivates a latent septin assembly pathway that was suppressed during fungal evolution in order to restrict assembly to octamers. Since homodimerization by a GTPase-active human septin also creates hexamers that exclude Cdc10-like central subunits, our new mechanistic insights likely apply throughout phylogeny.

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Published In

Elife

DOI

EISSN

2050-084X

Publication Date

January 28, 2020

Volume

9

Location

England

Related Subject Headings

  • Septins
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Hot Temperature
  • Guanidine
  • Biopolymers
  • Arginine
  • 42 Health sciences
  • 32 Biomedical and clinical sciences
  • 31 Biological sciences
 

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Johnson, C. R., Steingesser, M. G., Weems, A. D., Khan, A., Gladfelter, A., Bertin, A., & McMurray, M. A. (2020). Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast. Elife, 9. https://doi.org/10.7554/eLife.54355
Johnson, Courtney R., Marc G. Steingesser, Andrew D. Weems, Anum Khan, Amy Gladfelter, Aurélie Bertin, and Michael A. McMurray. “Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast.Elife 9 (January 28, 2020). https://doi.org/10.7554/eLife.54355.
Johnson CR, Steingesser MG, Weems AD, Khan A, Gladfelter A, Bertin A, et al. Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast. Elife. 2020 Jan 28;9.
Johnson, Courtney R., et al. “Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast.Elife, vol. 9, Jan. 2020. Pubmed, doi:10.7554/eLife.54355.
Johnson CR, Steingesser MG, Weems AD, Khan A, Gladfelter A, Bertin A, McMurray MA. Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast. Elife. 2020 Jan 28;9.

Published In

Elife

DOI

EISSN

2050-084X

Publication Date

January 28, 2020

Volume

9

Location

England

Related Subject Headings

  • Septins
  • Saccharomyces cerevisiae Proteins
  • Saccharomyces cerevisiae
  • Hot Temperature
  • Guanidine
  • Biopolymers
  • Arginine
  • 42 Health sciences
  • 32 Biomedical and clinical sciences
  • 31 Biological sciences