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Publication Abstract from PubMed

The Alba superfamily proteins have been regarded as a conserved group of proteins in archaea and eukarya, which have shown to be important in nucleic acid binding, chromatic organization and gene regulation. These proteins often belong to the N-acetyltransferase (NAT) category (N(alpha)-acetyltransferases or N(epsilon)-acetyltransferases) and undergo post-translational modifications. Here, we report the crystal structure of Alba from Thermoplasma volcanium (Tv Alba) at 2.4 A resolution. The acetylation of Tv Alba was monitored and the N-terminal of Tv Alba has been shown to interact with acetyl coenzyme A (Ac-CoA). The chemical shift perturbation experiments of Tv Alba were performed in the presence of Ac-CoA and/or Tv Ard1, another T. volcanium protein that treats Tv Alba as a substrate. To examine the DNA binding capabilities of Tv Alba alone and in the presence of Ac-CoA and/or Tv Ard1, EMSA experiments were carried out. It is shown that although Tv Alba binds to Ac-CoA, the acetylation of Tv Alba is not related with its binding to dsDNA, and the involvement of the N-terminus in Ac-CoA binding demonstrates that Tv Alba belongs to the N(alpha)-acetyltransferase family.

Alba from Thermoplasma volcanium belongs to alpha-NAT's: An insight into the structural aspects of Tv Alba and its acetylation by Tv Ard1.,Ma C, Pathak C, Lee SJ, Lee KY, Jang SB, Nam M, Im H, Yoon HJ, Lee BJ Arch Biochem Biophys. 2016 Jan 15;590:90-100. doi: 10.1016/j.abb.2015.11.039., Epub 2015 Nov 30. PMID:26657068^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.