Charged single alpha-helices in proteomes revealed by a consensus prediction approach

Z. Gáspári, Dániel Süveges, A. Perczel, L. Nyitray, Gábor Tóth

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)637-646
Number of pages10
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1824
Issue number4
DOIs
Publication statusPublished - Apr 2012

Fingerprint

Proteome
Proteins
Symbiosis
Conservation
Biological Phenomena
Amino Acid Motifs
Molecular Evolution
alpha-Helical Protein Conformation
Web services
Databases
RNA
Processing

Keywords

  • Charged single alpha-helix
  • Protein evolution
  • Structure prediction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

Cite this

Charged single alpha-helices in proteomes revealed by a consensus prediction approach. / Gáspári, Z.; Süveges, Dániel; Perczel, A.; Nyitray, L.; Tóth, Gábor.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1824, No. 4, 04.2012, p. 637-646.

Research output: Contribution to journalArticle

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