<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Siegrist, M Sloan</style></author><author><style face="normal" font="default" size="100%">Unnikrishnan, Meera</style></author><author><style face="normal" font="default" size="100%">McConnell, Matthew J</style></author><author><style face="normal" font="default" size="100%">Borowsky, Mark</style></author><author><style face="normal" font="default" size="100%">Cheng, Tan-Yun</style></author><author><style face="normal" font="default" size="100%">Siddiqi, Noman</style></author><author><style face="normal" font="default" size="100%">Fortune, Sarah M</style></author><author><style face="normal" font="default" size="100%">Moody, D Branch</style></author><author><style face="normal" font="default" size="100%">Rubin, Eric J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron</style></keyword><keyword><style  face="normal" font="default" size="100%">Macrophages</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxazoles</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Secretory Pathway</style></keyword><keyword><style  face="normal" font="default" size="100%">Siderophores</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Up-Regulation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Nov 3</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">106</style></volume><pages><style face="normal" font="default" size="100%">18792-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The Esx secretion pathway is conserved across Gram-positive bacteria. Esx-1, the best-characterized system, is required for virulence of Mycobacterium tuberculosis, although its precise function during infection remains unclear. Esx-3, a paralogous system present in all mycobacterial species, is required for growth in vitro. Here, we demonstrate that mycobacteria lacking Esx-3 are defective in acquiring iron. To compete for the limited iron available in the host and the environment, these organisms use mycobactin, high-affinity iron-binding molecules. In the absence of Esx-3, mycobacteria synthesize mycobactin but are unable to use the bound iron and are impaired severely for growth during macrophage infection. Mycobacteria thus require a specialized secretion system for acquiring iron from siderophores.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">44</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19846780?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Siegrist, M Sloan</style></author><author><style face="normal" font="default" size="100%">Rubin, Eric J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Phage transposon mutagenesis.</style></title><secondary-title><style face="normal" font="default" size="100%">Methods Mol Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Methods Mol. Biol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bacteriophages</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Transposable Elements</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutagenesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium</style></keyword><keyword><style  face="normal" font="default" size="100%">Transduction, Genetic</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">465</style></volume><pages><style face="normal" font="default" size="100%">311-23</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Phage transduction is an attractive method of genetic manipulation in mycobacteria. PhiMycoMarT7 is well suited for transposon mutagenesis as it is temperature sensitive for replication and contains T7 promoters that promote transcription, a highly active transposase gene, and an Escherichia coli oriR6 K origin of replication. Mycobacterial transposon mutant libraries produced by PhiMycoMarT7 transduction are amenable to both forward and reverse genetic studies. In this protocol, we detail the preparation of PhiMycoMarT7, including a description of the phage, reconstitution of the phage, purification of plaques, preparation of phage stock, and titering of phage stock. We then describe the transduction procedure and finally outline the isolation of individual transposon mutants.&lt;/p&gt;</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/20560067?dopt=Abstract</style></custom1></record></records></xml>