Alba from Thermoplasma volcanium belongs to alpha-NAT's: An insight into the structural aspects of Tv Alba and its acetylation by Tv Ard1

作者：Ma Chao; Pathak Chinar; Lee Sang Jae; Lee Ki Young; Jang Sun Bok; Nam Minjoo; Im Hookang; Yoon Hye Jin; Lee Bong Jin^*

来源：Archives of Biochemistry and Biophysics, 2016, 590: 90-100.

DOI：10.1016/j.abb.2015.11.039

• Thermoplasma volcanium
• Alba
• Ard1
• N-terminal acetyltransferase
• Crystallography
• NMR

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 angstrom 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.

• 出版日期2016-1-15