A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes
- PMID: 12801414
- PMCID: PMC193619
- DOI: 10.1186/gb-2003-4-6-r40
A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes
Abstract
We have derived a novel method to assess compositional biases in biological sequences, which is based on finding the lowest-probability subsequences for a given residue-type set. As a case study, the distribution of prion-like glutamine/asparagine-rich ((Q+N)-rich) domains (which are linked to amyloidogenesis) was assessed for budding and fission yeasts and four other eukaryotes. We find more than 170 prion-like (Q+N)-rich regions in budding yeast, and, strikingly, many fewer in fission yeast. Also, some residues, such as tryptophan or isoleucine, are unlikely to form biased regions in any eukaryotic proteome.
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References
-
- Harrison PM, Bamborough P, Daggett V, Prusiner SB, Cohen FE. The prion folding problem. Curr Opin Struct Biol. 1997;7:53–59. - PubMed
-
- Harrison PM, Chan HS, Prusiner SB, Cohen FE. Thermodynamics of model prions and its implications for the problem of prion protein folding. J Mol Biol. 1999;286:593–606. - PubMed
-
- Serio TR, Lindquist SL. Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol. 2000;10:98–105. - PubMed
-
- Wickner RB, Taylor KL, Edskes HK, Maddelein ML. Prions: portable prion domains. Curr Biol. 2000;10:R335–R337. - PubMed
-
- Wickner RB, Taylor KL, Edskes HK, Maddelein ML, Moriyama H, Roberts BT. Prions of yeast as heritable amyloidoses. J Struct Biol. 2000;130:310–322. - PubMed
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