Crystallization Of The N-Terminal Domain Of Dff45: The Mutual Chaperone Mechanism Is Challenged

Title: Crystallization Of The N-Terminal Domain Of Dff45: The Mutual Chaperone Mechanism Is Challenged

Volume: 10 Issue: 2

Author(s): T. Li, X. Li, W. Yang, Z. Rao and Zh. Zhai

Affiliation:

Keywords: dff45, dff40, terminal domain, crystallization, chaperone, dna fragmentation, apoptotic

Abstract: DNA fragmentation factor 45 (DFF45) regulates DNase DFF40 as its inhibitor and chaperone. It was reported that the N-terminal domain (NTD) of DFF45 alone is disordered and DFF40 is necessary as a mutual chaperone for the folding of NTD. However, here we reported the crystallization of DFF45 NTD. These crystals diffract to 9Å using a synchrotron radiation source. In spite of the low resolution, the demonstration of crystal formation indicates that DFF45 NTD itself is not unstructured, which strongly questions the mutual chaperone speculation about DFF45 and DFF40.

Cite this article as:

Li T., Li X., Yang W., Rao Z. and Zhai Zh., Crystallization Of The N-Terminal Domain Of Dff45: The Mutual Chaperone Mechanism Is Challenged, Protein & Peptide Letters 2003; 10 (2) . https://dx.doi.org/10.2174/0929866033479068