Crystallization of the N-terminal domain of DFF45: the mutual chaperone mechanism is challenged.

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 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.

journal_name

Protein Pept Lett

authors

Li T,Li X,Yang W,Rao Z,Zhai Zh

doi

10.2174/0929866033479068

subject

Has Abstract

pub_date

2003-04-01 00:00:00

pages

221-5

issue

2

eissn

0929-8665

issn

1875-5305

journal_volume

10

pub_type

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