Truncation of the caspase-related subunit (Gpi8p) of Saccharomyces cerevisiae GPI transamidase: Dimerization revealed
Abstract
Eukaryotic proteins can be post-translationally modified with a glycosylphosphatidylinositol (GPI) membrane anchor. This modification reaction is catalyzed by GPI transamidase (GPI-T), a multimeric, membrane-bound enzyme. Gpi8p, an essential component of GPI-T, shares low sequence similarity with caspases and contains all or part of the enzyme's active site [U. Meyer, M. Benghezal, I. Imhof, A. Conzelmann, Biochemistry 39 (2000) 3461-3471]. Structural predictions suggest that the soluble portion of Gpi8p is divided into two domains: a caspase-like domain that contains the active site machinery and a second, smaller domain of unknown function. Based on these predictions, we evaluated a soluble truncation of Gpi8p (Gpi8(23-306)). Dimerization was investigated due to the known proclivity of caspases to homodimerize; a Gpi8(23-306) homodimer was detected by native gel and confirmed by mass spectrometry and N-terminal sequencing. Mutations at the putative caspase-like dimerization interface disrupted dimer formation. When combined, these results demonstrate an organizational similarity between Gpi8p and caspases.
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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 [98]
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Computed structures of core eukaryotic protein complexes
Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542 · see citing works
Self-citationGPI Transamidase and GPI anchored proteins: Oncogenes and biomarkers for cancer
Gamage, D. G., & Hendrickson, T. L. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.831024 · Cited by 63 · see citing works
Self-citationYi, L., Bozkurt, G., Li, Q., Lo, S., Menon, A. K., & Wu, H. (2017) · Scientific Reports · doi:10.1038/srep45912 · Cited by 12 · see citing works
Gamage, D. G., Varma, Y., Meitzler, J. L., Morissette, R., Ness, T. J., & Hendrickson, T. L. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.09.006 · Cited by 8 · see citing works
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- Authors
- Meitzler, J. L., Gray, J. J., & Hendrickson, T. L.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Hendrickson, Tamara L.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2007-06
- Volume
- 462
- Issue
- 1
- Pages
- 83-93
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W1974739567
- Cited by
- 18
- References
- 76
- Citations by year
- 2026: 1 · 2025: 3 · 2022: 1 · 2021: 1 · 2017: 2 · 2015: 1 · 2014: 1 · 2013: 2
- FWCI
- 0.79
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- protein truncation, homodimerization, dimer interface, glycosylphosphatidylinositol anchor, Saccharomyces cerevisiae, protein structure, active site
- MeSH terms
- Amino Acid Sequence, Carbohydrate Sequence, Catalysis, Cytosol, Models, Chemical, Models, Molecular, Molecular Sequence Data, Mutation, Saccharomyces cerevisiae, Cell Adhesion Molecules, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Dimerization, Aminoacyltransferases, Caspases, Saccharomyces cerevisiae Proteins
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