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MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteins

Authors
Publisher
BioMed Central
Publication Date
Source
PMC
Keywords
  • Software
Disciplines
  • Biology
  • Medicine

Abstract

gb-2004-5-3-r21.fm co m m ent review s repo rts depo sited research refereed research interactio ns info rm atio Open Access2004Maurer-Strohet al.Volume 5, Issue 3, Article R21Software MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteins Sebastian Maurer-Stroh*, Masaki Gouda†, Maria Novatchkova*, Alexander Schleiffer*, Georg Schneider*, Fernanda L Sirota‡, Michael Wildpaner*, Nobuhiro Hayashi† and Frank Eisenhaber* Addresses: *IMP Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria. †Division of Biomedical Polymer Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan. ‡Service de Conformation de Macromolecules Biologiques et de Bioinformatique, Université Libre de Bruxelles, Boulevard du Triomphe - CP 263, 1050 Bruxelles, Belgium. Correspondence: Sebastian Maurer-Stroh. E-mail: [email protected] © 2004 Maurer-Stroh et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteinsWe evaluated the evolutionary conservation of glycine myristoylation within eukaryotic sequences. Our large-scale cross-genome analyses, available as MYRbase, show that the functional spectrum of myristoylated proteins is currently largely underestimated. We give experimen-tal evidence for in vitro myristoylation of selected predictions. Furthermore, we classify five membrane-attachment factors that occur most frequently in combination with, or even replacing, myristoyl anchors, as some protein family examples show. Abstract We evaluated the evolutionary conservation of glycine myristoylation within eukaryotic sequences. Our larg

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