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

doi:10.1186/gb-2004-5-3-r21

Genome Biology

Volume 5
Issue 3

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Maurer-Stroh S
Gouda M
Novatchkova M
Schleiffer A
Schneider G
Sirota FL
Wildpaner M
Hayashi N
Eisenhaber F

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Maurer-Stroh S
Gouda M
Novatchkova M
Schleiffer A
Schneider G
Sirota FL
Wildpaner M
Hayashi N
Eisenhaber F
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MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteins

Sebastian Maurer-Stroh¹ , Masaki Gouda², Maria Novatchkova¹, Alexander Schleiffer¹, Georg Schneider¹, Fernanda L Sirota³, Michael Wildpaner¹, Nobuhiro Hayashi² and Frank Eisenhaber¹

¹IMP Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria

²Division of Biomedical Polymer Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan

³Service de Conformation de Macromolecules Biologiques et de Bioinformatique, Université Libre de Bruxelles, Boulevard du Triomphe - CP 263, 1050 Bruxelles, Belgium

author email corresponding author email

Genome Biology 2004, 5:R21doi:10.1186/gb-2004-5-3-r21


Published:	13 February 2004

Subject areas: Biochemistry and structural biology, Bioinformatics, Cell biology, Evolution

Abstract

We 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 experimental 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.