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Identification of proteins interacting with GTP cyclohydrolase I. Biochem Biophys Res Commun 2009 Jul 24;385(2):143-7



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Pubmed Central ID




Scopus ID

2-s2.0-67349116808   8 Citations


GTP cyclohydrolase I (GCH-1) is the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin, an essential cofactor for nitric oxide synthase and aromatic amino acid hydroxylase. To explore the interactome of GCH-1, we established a HEK 293 cell line stably expressing tetracycline-inducible FLAG-GCH-1. FLAG-GCH-1 and associated proteins were immunoprecipitated and analyzed by liquid chromatography/tandem mass spectrometry. Twenty-nine proteins, derived from different subcellular components such as cytosol, membranes, nucleus and mitochondria were identified to interact with GCH-1. Cell fractionation studies also showed that GCH-1 was present in the cytosol, membranes and nucleus. Gene ontology analysis revealed that GCH-1 interactome was involved in a variety of biological processes such as signal transduction, apoptosis, metabolism, transport and cell organization. To our knowledge, this study is the first to provide a comprehensive analysis of the GCH-1 interactome. Findings expand the number and diversity of proteins that are known to associate with GCH-1.

Author List

Du J, Xu H, Wei N, Wakim B, Halligan B, Pritchard KA Jr, Shi Y


Kirkwood A. Pritchard PhD Professor in the Surgery department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Cell Fractionation
Cell Line
Cell Nucleus
Chromatography, Liquid
GTP Cyclohydrolase
Tandem Mass Spectrometry
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a