Charged single alpha-helices in proteomes revealed by a consensus prediction approach.
Charged single α-helices (CSAHs) constitute a recently recognized protein structural motif. Its presence and role is characterized in only a few proteins. To explore its general features, a comprehensive study is necessary. We have set up a consensus prediction method available as a web service (at http://csahserver.chem.elte.hu) and downloadable scripts capable of predicting CSAHs from protein sequences. Using our method, we have performed a comprehensive search on the UniProt database. We found that the motif is very rare but seems abundant in proteins involved in symbiosis and RNA binding/processing. Although there are related proteins with CSAH segments, the motif shows no deep conservation in protein families. We conclude that CSAH-containing proteins, although rare, are involved in many key biological processes. Their conservation pattern and prevalence in symbiosis-associated proteins suggest that they might be subjects of relatively rapid molecular evolution and thus can contribute to the emergence of novel functions.
Institute of Chemistry, Eötvös Loránd University, Budapest, Hungary. gaspari.zoltan@itk.ppke.hu
Zoltán
Z
Gáspári
Dániel
D
Süveges
András
A
Perczel
László
L
Nyitray
Gábor
G
Tóth
D000595:Amino Acid Sequence; D000818:Animals; D016384:Consensus Sequence; D030562:Databases, Protein; D019143:Evolution, Molecular; D006801:Humans; D008958:Models, Molecular; D058977:Molecular Sequence Annotation; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics; D017433:Protein Structure, Secondary; D020543:Proteome / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D012984:Software
D020033:Protein Isoforms; D020543:Proteome