@article {522,
	title = {DNA microarray and proteomic analyses of the RpoS regulon in Geobacter sulfurreducens.},
	journal = {J Bacteriol},
	volume = {188},
	year = {2006},
	month = {2006 Apr},
	pages = {2792-800},
	abstract = {The regulon of the sigma factor RpoS was defined in Geobacter sulfurreducens by using a combination of DNA microarray expression profiles and proteomics. An rpoS mutant was examined under steady-state conditions with acetate as an electron donor and fumarate as an electron acceptor and with additional transcriptional profiling using Fe(III) as an electron acceptor. Expression analysis revealed that RpoS acts as both a positive and negative regulator. Many of the RpoS-dependent genes determined play roles in energy metabolism, including the tricarboxylic acid cycle, signal transduction, transport, protein synthesis and degradation, and amino acid metabolism and transport. As expected, RpoS activated genes involved in oxidative stress resistance and adaptation to nutrient limitation. Transcription of the cytochrome c oxidase operon, necessary for G. sulfurreducens growth using oxygen as an electron acceptor, and expression of at least 13 c-type cytochromes, including one previously shown to participate in Fe(III) reduction (MacA), were RpoS dependent. Analysis of a subset of the rpoS mutant proteome indicated that 15 major protein species showed reproducible differences in abundance relative to those of the wild-type strain. Protein identification using mass spectrometry indicated that the expression of seven of these proteins correlated with the microarray data. Collectively, these results indicate that RpoS exerts global effects on G. sulfurreducens physiology and that RpoS is vital to G. sulfurreducens survival under conditions typically encountered in its native subsurface environments.},
	keywords = {Adaptation, Physiological, Amino Acids, Bacterial Proteins, Biological Transport, Citric Acid Cycle, Cytochromes, Electrophoresis, Gel, Two-Dimensional, Gene Deletion, Gene Expression Regulation, Bacterial, Geobacter, Mass Spectrometry, Mutagenesis, Insertional, Oligonucleotide Array Sequence Analysis, Oxidative Stress, Protein Biosynthesis, Proteome, Regulon, Sigma Factor, Signal Transduction},
	issn = {0021-9193},
	doi = {10.1128/JB.188.8.2792-2800.2006},
	author = {N{\'u}{\~n}ez, Cinthia and Esteve-N{\'u}{\~n}ez, Abraham and Giometti, Carol and Tollaksen, Sandra and Khare, Tripti and Lin, Winston and Lovley, Derek R and Meth{\'e}, Barbara A}
}
@article {718,
	title = {Simian virus 40 late proteins possess lytic properties that render them capable of permeabilizing cellular membranes.},
	journal = {J Virol},
	volume = {80},
	year = {2006},
	month = {2006 Jul},
	pages = {6575-87},
	abstract = {Many nonenveloped viruses have evolved an infectious cycle that culminates in the lysis or permeabilization of the host to enable viral release. How these viruses initiate the lytic event is largely unknown. Here, we demonstrated that the simian virus 40 progeny accumulated at the nuclear envelope prior to the permeabilization of the nuclear, endoplasmic reticulum, and plasma membranes at a time which corresponded with the release of the progeny. The permeabilization of these cellular membranes temporally correlated with late protein expression and was not observed upon the inhibition of their synthesis. To address whether one or more of the late proteins possessed an inherent capacity to induce membrane permeabilization, we examined the permeability of Escherichia coli that separately expressed the late proteins. VP2 and VP3, but not VP1, caused the permeabilization of bacterial membranes. Additionally, VP3 expression resulted in bacterial cell lysis. These findings demonstrate that VP3 possesses an inherent lytic property that is independent of eukaryotic signaling or cell death pathways.},
	keywords = {Animals, Capsid Proteins, Cell Death, Cell Line, Cell Membrane Permeability, Cercopithecus aethiops, Endoplasmic Reticulum, Escherichia coli, Gene Expression Regulation, Viral, Nuclear Envelope, Permeability, Protein Biosynthesis, Simian virus 40, Virus Replication},
	issn = {0022-538X},
	doi = {10.1128/JVI.00347-06},
	author = {Daniels, Robert and Rusan, Nasser M and Wilbuer, Anne-Kathrin and Norkin, Leonard C and Wadsworth, Patricia and Hebert, Daniel N}
}
@article {840,
	title = {Mutational analysis of sequences in the recF gene of Escherichia coli K-12 that affect expression.},
	journal = {J Bacteriol},
	volume = {176},
	year = {1994},
	month = {1994 Jul},
	pages = {4011-6},
	abstract = {The level of translation of recF-lacZ fusions is reduced 20-fold by nucleotides 49 to 146 of recF. In this region of recF, we found a previously described ribosome-interactive sequence called epsilon and a hexapyrimidine tract located just upstream of the epsilon sequence. Mutational studies indicate that the hexapyrimidine sequence is involved in at least some of the reduced translation. When the hexapyrimidine sequence is mutant, mutating epsilon increases the level of translation maximally. We ruled out the possibility that ribosome frameshifting explains most of the effect of these two sequences on expression and suspect that multiple mechanisms may be responsible. In a separate report, we show that mutations in the hexapyrimidine tract and epsilon increase expression of the full-sized recF gene.},
	keywords = {Bacterial Proteins, Base Sequence, DNA Mutational Analysis, DNA-Binding Proteins, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Genes, Bacterial, Half-Life, Lac Operon, Molecular Sequence Data, Protein Biosynthesis, Recombinant Fusion Proteins, Regulatory Sequences, Nucleic Acid, Ribosomes},
	issn = {0021-9193},
	author = {Sandler, S J and Clark, A J}
}
@article {847,
	title = {Genes of the RecE and RecF pathways of conjugational recombination in Escherichia coli.},
	journal = {Cold Spring Harb Symp Quant Biol},
	volume = {49},
	year = {1984},
	month = {1984},
	pages = {453-62},
	keywords = {Chromosome Mapping, Conjugation, Genetic, Escherichia coli, Genes, Bacterial, Mutation, Protein Biosynthesis, Recombination, Genetic},
	issn = {0091-7451},
	author = {Clark, A J and Sandler, S J and Willis, D K and Chu, C C and Blanar, M A and Lovett, S T}
}
