@article {462,
	title = {Anode biofilm transcriptomics reveals outer surface components essential for high density current production in Geobacter sulfurreducens fuel cells.},
	journal = {PLoS One},
	volume = {4},
	year = {2009},
	month = {2009},
	pages = {e5628},
	abstract = {The mechanisms by which Geobacter sulfurreducens transfers electrons through relatively thick (>50 microm) biofilms to electrodes acting as a sole electron acceptor were investigated. Biofilms of Geobacter sulfurreducens were grown either in flow-through systems with graphite anodes as the electron acceptor or on the same graphite surface, but with fumarate as the sole electron acceptor. Fumarate-grown biofilms were not immediately capable of significant current production, suggesting substantial physiological differences from current-producing biofilms. Microarray analysis revealed 13 genes in current-harvesting biofilms that had significantly higher transcript levels. The greatest increases were for pilA, the gene immediately downstream of pilA, and the genes for two outer c-type membrane cytochromes, OmcB and OmcZ. Down-regulated genes included the genes for the outer-membrane c-type cytochromes, OmcS and OmcT. Results of quantitative RT-PCR of gene transcript levels during biofilm growth were consistent with microarray results. OmcZ and the outer-surface c-type cytochrome, OmcE, were more abundant and OmcS was less abundant in current-harvesting cells. Strains in which pilA, the gene immediately downstream from pilA, omcB, omcS, omcE, or omcZ was deleted demonstrated that only deletion of pilA or omcZ severely inhibited current production and biofilm formation in current-harvesting mode. In contrast, these gene deletions had no impact on biofilm formation on graphite surfaces when fumarate served as the electron acceptor. These results suggest that biofilms grown harvesting current are specifically poised for electron transfer to electrodes and that, in addition to pili, OmcZ is a key component in electron transfer through differentiated G. sulfurreducens biofilms to electrodes.},
	keywords = {Amino Acid Sequence, Bacterial Outer Membrane Proteins, Bioelectric Energy Sources, Biofilms, Cytochromes, Electrodes, Electron Transport, Fumarates, Gene Deletion, Gene Expression Profiling, Gene Expression Regulation, Bacterial, Genetic Complementation Test, Geobacter, Microscopy, Confocal, Molecular Sequence Data, Oligonucleotide Array Sequence Analysis, Oxidation-Reduction, RNA, Messenger, Up-Regulation},
	issn = {1932-6203},
	doi = {10.1371/journal.pone.0005628},
	author = {Nevin, Kelly P and Kim, Byoung-Chan and Glaven, Richard H and Johnson, Jessica P and Woodard, Trevor L and Meth{\'e}, Barbara A and Didonato, Raymond J and Covalla, Sean F and Franks, Ashley E and Liu, Anna and Lovley, Derek R}
}
@article {1447,
	title = {Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {106},
	year = {2009},
	month = {2009 Nov 3},
	pages = {18792-7},
	abstract = {<p>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.</p>},
	keywords = {Animals, Bacterial Proteins, Genome, Bacterial, Iron, Macrophages, Mice, Mutation, Mycobacterium, Mycobacterium Infections, Oxazoles, Protein Binding, Secretory Pathway, Siderophores, Transcription, Genetic, Up-Regulation},
	issn = {1091-6490},
	doi = {10.1073/pnas.0900589106},
	author = {Siegrist, M Sloan and Unnikrishnan, Meera and McConnell, Matthew J and Borowsky, Mark and Cheng, Tan-Yun and Siddiqi, Noman and Fortune, Sarah M and Moody, D Branch and Rubin, Eric J}
}
@article {707,
	title = {Extracellular simian virus 40 induces an ERK/MAP kinase-independent signalling pathway that activates primary response genes and promotes virus entry.},
	journal = {J Gen Virol},
	volume = {77 ( Pt 9)},
	year = {1996},
	month = {1996 Sep},
	pages = {2173-82},
	abstract = {Simian virus 40 (SV40) binding to growth-arrested cells activated an intracellular signalling pathway that induced the up-regulation of the primary response genes c-myc, c-jun and c-sis within 30 min and of JE within 90 min. The up-regulation of the primary response genes occurred in the presence of cycloheximide and when UV-inactivated SV40 was adsorbed to cells. SV40 binding did not activate Raf or mitogen-activated protein kinase (MAP/ERK1), or mobilize intracellular Ca2+. The SV40-induced up-regulation of c-myc and c-jun was blocked by the tyrosine kinase inhibitor, genistein, and by the protein kinase C (PKC) inhibitor, calphostin C, but not by expression of the MAP kinase-specific phosphatase, MKP-1. These results suggest that the SV40-induced signalling pathway includes the activities of a tyrosine kinase and a Ca(2+)-independent isoform of PKC, but not of Raf or MAP kinase. Finally, SV40 infectious entry into cells was specifically and reversibly blocked by genistein.},
	keywords = {Animals, Calcium, Calcium-Calmodulin-Dependent Protein Kinases, Cell Cycle Proteins, Cell Line, Cercopithecus aethiops, Dual Specificity Phosphatase 1, Enzyme Inhibitors, Gene Expression Regulation, Viral, Genistein, Humans, Immediate-Early Proteins, Isoflavones, Mitogen-Activated Protein Kinase 3, Mitogen-Activated Protein Kinases, Naphthalenes, Phosphoprotein Phosphatases, Platelet-Derived Growth Factor, Protein Kinase C, Protein Phosphatase 1, Protein Tyrosine Phosphatases, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-jun, Proto-Oncogene Proteins c-myc, Proto-Oncogene Proteins c-raf, Proto-Oncogene Proteins c-sis, Signal Transduction, Simian virus 40, Up-Regulation},
	issn = {0022-1317},
	author = {Dangoria, N S and Breau, W C and Anderson, H A and Cishek, D M and Norkin, L C}
}
