Disulfide Bonding in Thermophilic Archaea
Author Information
Author(s): Jorda Julien, Yeates Todd O.
Primary Institution: UCLA-DOE Institute for Genomics and Proteomics
Hypothesis
How are thermophilic proteins stabilized in extreme environments?
Conclusion
Disulfide bonds are commonly used for protein stabilization in thermophilic archaea, particularly in the Crenarchaea group.
Supporting Evidence
- Disulfide bonding is a major mechanism for protein stabilization in thermophilic archaea.
- Crenarchaea are universally rich in disulfide bonding.
- The study utilized genomic data from 90 archaeal proteomes to assess disulfide bonding.
- Disulfide bonding is less abundant in Euryarchaea and absent in methanogenic species.
Takeaway
Some tiny organisms that live in really hot places use special bonds to keep their proteins from falling apart.
Methodology
The study analyzed protein sequences from 90 complete archaeal proteomes and applied computational methods to estimate disulfide bonding.
Potential Biases
Potential biases in cysteine counting due to metalloproteins and the presence of proteins with odd numbers of cysteines.
Limitations
The computational methods provide rough estimates of disulfide abundance and may underestimate actual levels due to various factors.
Participant Demographics
The study focused on 90 archaeal species, primarily from the Crenarchaeal and Euryarchaeal branches.
Digital Object Identifier (DOI)
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