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1.
Appl Environ Microbiol ; 68(10): 4764-71, 2002 Oct.
Article in English | MEDLINE | ID: mdl-12324318

ABSTRACT

Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) is a high explosive which presents an environmental hazard as a major land and groundwater contaminant. Rhodococcus rhodochrous strain 11Y was isolated from explosive contaminated land and is capable of degrading RDX when provided as the sole source of nitrogen for growth. Products of RDX degradation in resting-cell incubations were analyzed and found to include nitrite, formaldehyde, and formate. No ammonium was excreted into the medium, and no dead-end metabolites were observed. The gene responsible for the degradation of RDX in strain 11Y is a constitutively expressed cytochrome P450-like gene, xplA, which is found in a gene cluster with an adrenodoxin reductase homologue, xplB. The cytochrome P450 also has a flavodoxin domain at the N terminus. This study is the first to present a gene which has been identified as being responsible for RDX biodegradation. The mechanism of action of XplA on RDX is thought to involve initial denitration followed by spontaneous ring cleavage and mineralization.


Subject(s)
Rhodococcus/genetics , Triazines/metabolism , Amino Acid Sequence , Biodegradation, Environmental , Cloning, Molecular , Gene Expression Regulation, Bacterial , Molecular Sequence Data , Nitrogen/metabolism , Rhodococcus/growth & development , Rhodococcus/metabolism , Sequence Homology, Amino Acid , Soil Microbiology , Soil Pollutants/metabolism , Triazines/chemistry
2.
Biochim Biophys Acta ; 1564(1): 73-81, 2002 Aug 19.
Article in English | MEDLINE | ID: mdl-12100998

ABSTRACT

Potent cytolytic peptides with specific tethering and cloaking sites have been synthesised and used to release payload from liposomes in a quantitative manner. A functionally located cloaking site has been modified specifically by simple conjugation without adversely affecting the cytolytic properties of the peptide. The cytolytic activity of modified peptides was then efficiently (>98%) cloaked and uncloaked by ligand-protein or hapten-antibody interactions. The principle of a dual response peptide has been demonstrated using an avidin-cloaked pH-sensitive peptide. Biospecific cloaking/uncloaking provided a new sensitive (approximately 12 pmol) homogeneous diagnostic and also appears potentially suited to bioresponsively targeted release of antimicrobial, anticancer and other drugs now delivered using liposomes.


Subject(s)
Cytotoxins/administration & dosage , Peptides/administration & dosage , Amino Acid Sequence , Avidin , Biotin , Cytotoxins/chemical synthesis , Drug Delivery Systems , Hydrogen-Ion Concentration , Liposomes , Melitten/administration & dosage , Melitten/chemical synthesis , Molecular Sequence Data , Peptides/chemical synthesis
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