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


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.

SUBMITTER: Maurer-Stroh S 

PROVIDER: S-EPMC395771 | biostudies-literature | 2004

REPOSITORIES: biostudies-literature

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

Maurer-Stroh Sebastian S   Gouda Masaki M   Novatchkova Maria M   Schleiffer Alexander A   Schneider Georg G   Sirota Fernanda L FL   Wildpaner Michael M   Hayashi Nobuhiro N   Eisenhaber Frank F  

Genome biology 20040213 3


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 f  ...[more]

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