Journal article icon

Journal article

Destabilization of the colicin E9 Endonuclease domain by interaction with negatively charged phospholipids: implications for colicin translocation into bacteria.

Abstract:

We have shown previously that the 134-residue endonuclease domain of the bacterial cytotoxin colicin E9 (E9 DNase) forms channels in planar lipid bilayers (Mosbahi, K., Lemaître, C., Keeble, A. H., Mobasheri, H., Morel, B., James, R., Moore, G. R., Lea, E. J., and Kleanthous, C. (2002) Nat. Struct. Biol. 9, 476-484). It was proposed that the E9 DNase mediates its own translocation across the cytoplasmic membrane and that the formation of ion channels is essential to this process. Here we desc...

Expand abstract

Actions


Access Document


Publisher copy:
10.1074/jbc.m400402200

Authors


Expand authors...
Journal:
The Journal of biological chemistry
Volume:
279
Issue:
21
Pages:
22145-22151
Publication date:
2004-05-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:610ea33a-322e-47a3-9088-a9d372e824de
Source identifiers:
310187
Local pid:
pubs:310187

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP