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Cited by 8Glycosylation and Glycoproteins ResearchFungal and yeast genetics researchCellular transport and secretion

The soluble domains of Gpi8 and Gaa1, two subunits of glycosylphosphatidylinositol transamidase (GPI-T), assemble into a complex

Gamage, Dilani G., Varma, Yug, Meitzler, Jennifer L., Morissette, Rachel, Ness, Travis J., Hendrickson, Tamara L.·2017·Archives of Biochemistry and Biophysics
DOI 10.1016/j.abb.2017.09.006
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Abstract

Glycosylphosphatidylinositol transamidase (GPI-T) catalyzes the post-translational addition of the GPI anchor to the C-terminus of some proteins. In most eukaryotes, Gpi8, the active site subunit of GPI-T, is part of a hetero-pentameric complex containing Gpi16, Gaa1, Gpi17, and Gab1. Gpi8, Gaa1, and Gpi16 co-purify as a heterotrimer from Saccharomyces cerevisiae, suggesting that they form the core of the GPI-T. Details about the assembly and organization of these subunits have been slow to emerge. We have previously shown that the soluble domain of S. cerevisiae Gpi8 (Gpi8 23-306) assembles as a homodimer, similar to the caspases with which it shares weak sequence homology (Meitzler, J. L. et al., 2007). Here we present the characterization of a complex between the soluble domains of Gpi8 and Gaa1. The complex between GST-Gpi8 23-306 (α) and His 6-Gaa1 50-343 (β) was characterized by native gel analysis and size exclusion chromatography (SEC) and results are most consistent with an α 2 β 2 stoichiometry. These results demonstrate that Gpi8 and Gaa1 interact specifically without a requirement for other subunits, bring us closer to determining the stoichiometry of the core subunits of GPI-T, and lend further credence to the hypothesis that these three subunits assemble into a dimer of a trimer.

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  • In vivo, GPI-T is expected to be a dimer of pentamers, with dimerization occurring on one face of the caspase-like Gpi8 subunit.

    “In vivo, GPI-T is expected to be a dimer of pentamers, with dimerization occurring on one face of the caspase-like Gpi8 subunit (92,97,98).”

    From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [97]

  • The highly conserved face of Gaa1 is proposed to recognize GPI anchor glycans.

    “proposed to recognize the GPI anchor glycans (96,97).”

    From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [97]

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Authors
Gamage, D. G., Varma, Y., Meitzler, J. L., Morissette, R., Ness, T. J., & Hendrickson, T. L.
Affiliations
  • Wayne State University (US)
  • Johns Hopkins University (US)
Corresponding author
Hendrickson, Tamara L.
ORCID
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
2017-11
Volume
633
Pages
58-67
ISSN
0003-9861 (ISSN-L)
DOI
10.1016/j.abb.2017.09.006
OpenAlex
W2752622236
Cited by
8
References
65
Citations by year
2025: 1 · 2024: 1 · 2022: 2 · 2021: 1 · 2020: 2 · 2018: 1
FWCI
0.33
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Archives of Biochemistry and Biophysics (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • American Cancer Society (RSG-07-217-01 to T. L. H.)
  • Wayne State University
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
soluble domain, protein-protein interaction, subunit stoichiometry, Saccharomyces cerevisiae
MeSH terms
Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Binding Sites, Cloning, Molecular, Escherichia coli, Kinetics, Membrane Glycoproteins, Models, Molecular, Protein Binding, Recombinant Proteins, Saccharomyces cerevisiae, Solubility, Substrate Specificity, Vibrionaceae, Gene Expression, Protein Structure, Tertiary, Aminoacyltransferases, Amino Acid Motifs, Saccharomyces cerevisiae Proteins, Structural Homology, Protein, Protein Interaction Domains and Motifs, Protein Multimerization

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