Crystallization of the N-terminal domain of DFF45: the mutual chaperone mechanism is challenged.
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 9A 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.
Li
T
T
Laboratory of Structural Biology, School of Life Sciences and Engineering Tsinghua University, Beijing 100084, China.
Li
X
X
Yang
W
W
Rao
Z
Z
Zhai
Zh
Zh
D051017:Apoptosis Regulatory Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D003851:Deoxyribonucleases / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D018832:Molecular Chaperones / Q000378:metabolism*; D000075223:Poly-ADP-Ribose Binding Proteins; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism
D051017:Apoptosis Regulatory Proteins; D047908:Intracellular Signaling Peptides and Proteins; D018832:Molecular Chaperones; D000075223:Poly-ADP-Ribose Binding Proteins; D011506:Proteins; C109664:caspase-activated DNase inhibitor; C113696:DFFB protein, human; D003851:Deoxyribonucleases