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School of Biological Sciences: Faculty Publications
Biotin; domains; holocarboxylase synthetase; substrate; Syn67
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The Polypeptide Syn67 Interacts Physically With Human Holocarboxylase Synthetase, But Is Not A Target For Biotinylation, Yousef I. Hassan, Hideaki Moriyama, Janos Zempleni
The Polypeptide Syn67 Interacts Physically With Human Holocarboxylase Synthetase, But Is Not A Target For Biotinylation, Yousef I. Hassan, Hideaki Moriyama, Janos Zempleni
School of Biological Sciences: Faculty Publications
Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5′-AMP; second, the biotinyl moiety is ligated to lysine residues. It has been proposed that step two is fairly promiscuous, and that protein biotinylation may occur in the absence of HCS as long as sufficient exogenous biotinyl-5′- AMP is provided. Here, we identified a novel polypeptide (Syn67) with a basic patch of lysines and arginines. Yeast-two-hybrid assays and limited proteolysis assays revealed that both N- and C-termini of HCS interact with Syn67. A potential target lysine in …