ArticleThe Journal of biological chemistry2012
Crystal structure of the yeast metacaspase Yca1.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 94 citations in OpenAlex.
- The structural, functional, and therapeutic potential of metacaspases in fungi and protozoa.The FEBS journal · 2026Review
- The Activity of YCA1 Metacaspase Is Regulated by Reactive Sulfane Sulfur via Persulfidation inAntioxidants (Basel, Switzerland) · 2024Article
- Thermoprotection by a cell membrane-localized metacaspase in a green alga.The Plant cell · 2024Article
- Specifically Targeting Metacaspases ofJournal of fungi (Basel, Switzerland) · 2024Review
- Arabidopsis metacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence.The Plant cell · 2023Article
- Caspase 3 exhibits a yeast metacaspase proteostasis function that protects mitochondria from toxic TDP43 aggregates.Microbial cell (Graz, Austria) · 2023Article
- Structure-function study of a CaProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Yca1 metacaspase: diverse functions determine how yeast live and let die.FEMS yeast research · 2023Article
- Regulating Death and Disease: Exploring the Roles of Metacaspases in Plants and Fungi.International journal of molecular sciences · 2022Review
- Article
- Structural and molecular determinants of Candida glabrata metacaspase maturation and activation by calcium.Communications biology · 2022Article
- Roles of the pro-apoptotic factors CaNma111 and CaYbh3 in apoptosis and virulence of Candida albicans.Scientific reports · 2022Article
- Evolutionary Diversity and Function of Metacaspases in Plants: Similar to but Not Caspases.International journal of molecular sciences · 2022Review
- A Peptide Derived from GAPDH Enhances Resistance to DNA Damage in Saccharomyces cerevisiae Cells.Applied and environmental microbiology · 2022Article
- Expression and Purification of the Type I Metacaspase from a Cryptophyte Guillardia theta , GtMCA-I.Methods in molecular biology (Clifton, N.J.) · 2022Article
- A Systematic Survey of Characteristic Features of Yeast Cell Death Triggered by External Factors.Journal of fungi (Basel, Switzerland) · 2021Review
- TwinCons: Conservation score for uncovering deep sequence similarity and divergence.PLoS computational biology · 2021Article
- Article
- Bioinformatic mapping of a more precise Aspergillus niger degradome.Scientific reports · 2021Article
- Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon.Memorias do Instituto Oswaldo Cruz · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yca1, the only metacaspase in Saccharomyces cerevisiae, is thought to be a clan CD cysteine protease that includes the caspase subfamily. Although yeast is a single cell eukaryote, it can undergo a cell death process reminiscent of apoptosis. Yca1 has been reported to play an important role in the regulation of such apoptotic process. However, the structure and functional mechanism of Yca1 remain largely enigmatic. In this study, we report the crystal structure of the Yca1 metacaspase at 1.7 Å resolution, confirming a caspase-like fold. In sharp contrast to canonical caspases, however, Yca1 exists as a monomer both in solution and in the crystals. Canonical caspase contains six β-strands, with strand β6 pairing up with β6 of another caspase molecule to form a homodimerization interface. In Yca1, an extra pair of antiparallel β-strands forms a continuous β-sheet with the six caspase-common β-strands, blocking potential dimerization. Yca1 was reported to undergo autocatalytic processing in yeast; overexpression in bacteria also led to autoprocessing of Yca1 into two fragments. Unexpectedly, we found that both the autocatalytic processing and the proteolytic activity of Yca1 are greatly facilitated by the presence of calcium (Ca(2+)), but not other divalent cations. Our structural and biochemical characterization identifies Yca1 as a Ca(2+)-activated cysteine protease that may cleave specific substrates during stress response in yeast.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.