EcoliWiki - User contributions [en]

PMID:400782

2013-06-10T18:05:42Z

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'''Bagdasarian, MM, Izakowska, M and Bagdasarian, M''' (1977) Suppression of the DnaA phenotype by mutations in the rpoB cistron of ribonucleic acid polymerase in Salmonella typhimurium and Escherichia coli. ''J. Bacteriol.'' '''130''':577-82
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!align=left |Abstract
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A class of mutations that confer resistance to rifampin in Salmonella typhimurium and Escherichia coli also suppresses the thermosensitivity of chromosome initiation in dnaA mutants. Ribonucleic acid polymerase is resistant to rifampin in vitro in these suppressive mutants, and the suppressors of dnaA cannot be separated from the rpoB mutations by transduction. It is concluded, therefore, that certain rpoB mutations may suppress the DnaA phenotype.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=400782 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC235255 PMC235255]

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!align=left |Keywords
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DNA Replication; DNA-Directed RNA Polymerases/analysis; DNA-Directed RNA Polymerases/genetics; Drug Resistance, Microbial; Escherichia coli/genetics; Genes; Genes, Bacterial; Mutation; Rifampin/pharmacology; Salmonella typhimurium/genetics; Suppression, Genetic

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PMID:400782

2013-06-10T18:05:42Z

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PMID:23192655

2012-11-30T23:41:50Z

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'''Chen, S, Zhang, J, Lumley, L and Cashman, JR''' (2012) Immunodetection of Serum Albumin Adducts as Biomarkers for Organophosphorus Exposure.''J. Pharmacol. Exp. Ther.''
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!align=left |Abstract
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A major challenge in organophosphate (OP) research has been the identification and utilization of reliable biomarkers for the rapid, sensitive and efficient detection of OP exposure. Although tyrosine (Tyr) 411 OP adducts to human serum albumin (HSA) have been suggested to be one of the most robust biomarkers in the detection of OP exposure, the analysis of HSA-OP adduct detection has been limited to techniques using mass spectrometry. Herein, we describe the procurement of two monoclonal antibodies (mAb-HSA-GD and mAb-HSA-VX) that recognized the HSA Tyr 411 adduct of soman (GD) or VX, respectively, but did not recognize non-phosphonylated HSA. We showed that mAb-HSA-GD was able to detect the HSA Tyr 411 OP adduct at a low level (i.e., human blood plasma treated with 180 nM soman) that could not be detected by mass spectrometry. mAb-HSA-GD and mAb-HSA-VX showed an extremely low level detection of GD-adducted to HSA (on the order of picograms or 10-12 g). mAb-HSA-GD could also detect serum albumin OP adducts in blood plasma samples from different animals administered GD including rat, guinea pig and monkey. The ability of the two antibodies to selectively recognize nerve agents adducted to serum albumin suggests that these antibodies could be used to identify biomarkers of OP exposure and provide a new biological approach to detect OP exposure in animals.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=23192655 PubMed]
Online version:[http://dx.doi.org/10.1124/jpet.112.201368 10.1124/jpet.112.201368]
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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{| id="U50b9443e49555" class=" tableEdit GO_table_reference dataTable"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:23192655

2012-11-30T23:41:50Z

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PMID:20596754

2012-11-30T23:32:45Z

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'''Chu, BC, Garcia-Herrero, A, Johanson, TH, Krewulak, KD, Lau, CK, Peacock, RS, Slavinskaya, Z and Vogel, HJ''' (2010) Siderophore uptake in bacteria and the battle for iron with the host; a bird's eye view.''Biometals'' '''23''':601-11
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!align=left |Abstract
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Siderophores are biosynthetically produced and secreted by many bacteria, yeasts, fungi and plants, to scavenge for ferric iron (Fe(3+)). They are selective iron-chelators that have an extremely high affinity for binding this trivalent metal ion. The ferric ion is poorly soluble but it is the form of iron that is predominantly found in oxygenated environments. Siderophore uptake in bacteria has been extensively studied and over the last decade, detailed structural information for many of the proteins that are involved in their transport has become available. Specifically, numerous crystal structures for outer membrane siderophore transporters, as well as for soluble periplasmic siderophore-binding proteins, have been reported. Moreover, unique siderophore-binding proteins have recently been serendipitously discovered in humans, and the structures of some of their siderophore-complexes have been characterized. The binding pockets for different ferric-siderophores in these proteins have been described in great molecular detail. In addition to highlighting this structural information, in this review paper we will also briefly discuss the relevant chemical properties of iron, and provide a perspective on our current understanding of the human and bacterial iron uptake pathways. Potential clinical uses of siderophores will also be discussed. The emerging overall picture is that iron metabolism plays an extremely important role during bacterial infections. Because levels of free ferric iron in biological systems are always extremely low, there is serious competition for iron and for ferric-siderophores between pathogenic bacteria and the human or animal host.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20596754 PubMed]
Online version:[http://dx.doi.org/10.1007/s10534-010-9361-x 10.1007/s10534-010-9361-x]
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Animals; Bacteria; Humans; Immunity, Innate; Iron; Iron Chelating Agents; Lipocalins; Models, Molecular; Protein Conformation; Siderophores

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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<protect>

{| id="M50b9421d47a66" class=" tableEdit GO_table_reference dataTable"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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</protect>

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PMID:20596754

2012-11-30T23:32:44Z

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PMID:6450313

2012-03-19T20:09:31Z

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'''Lengeler, J''' (1980) Characterisation of mutants of Escherichia coli K12, selected by resistance to streptozotocin.''Mol. Gen. Genet.'' '''179''':49-54
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!align=left |Abstract
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From cultures of sensitive bacteria, treated with the antibiotic streptozotocin, two classes of resistant mutants can be isolated: 1) mutants, resistant under all the conditions tested to even the highest doses of the antibiotic. These are either pleiotropic-defective, pts-mutants, or more frequently, mutants lacking a transport system (enzyme IINag-complex of the PEP-dependent phosphotransferase system) encoded by the gene nagE. This gene is inducible by N-acetyl-glucosamine and seems to be part of the nag operon. The transport system in question is responsible for the uptake of N-acetyl-glucosamine, of D-glucosamine and of streptozotocin; 2) conditional resistant mutants which are unable to energize or to synthesize the streptozotocin transport system under certain growth conditions but do have the transport activity under other conditions. These include a) mutants auxotrophic for amino acids, vitamins, or nucleotides, b) mutants negative or sensitive to carbohydrates in the medium, and c) mutants wth defects in energy metabolism such as PEP synthesis.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6450313 PubMed]

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Dose-Response Relationship, Drug; Drug Resistance, Microbial; Escherichia coli; Mutation; Phenotype; Streptozocin

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{| id="E4f67927b8ac47" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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<references/>

PMID:6450313

2012-03-19T20:09:20Z

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PMID:7005898

2011-02-24T22:05:05Z

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<protect>
 '''Herlihy, WC, Royal, NJ, Biemann, K, Putney, SD and Schimmel, PR''' (1980) Mass spectra of partial protein hydrolysates as a multiple phase check for long polypeptides deduced from DNA sequences: NH2-terminal segment of alanine tRNA synthetase.''Proc. Natl. Acad. Sci. U.S.A.'' '''77''':6531-5

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|{{TableHeadingColor}} |'''Abstract''' || <protect>A strategy has been developed for rapid and accurate determination of the amino acid sequence of large proteins, such as many of the members of the class of proteins known as aminoacyl tRNA synthetases. This strategy involves combining DNA sequencing of the gene for the protein of interest with gas chromatographic mass spectrometric identification of tetra- and pentapeptides in partial hydrolysates of the entire protein or very large fragments thereof. These peptides are matched to blocks of codons at locations scattered throughout the entire structural gene. Tetra- and pentapeptide sequences are sufficiently long that they are unlikely to be repeated in the protein sequence or to occur in an incorrect reading frame; therefore, they can be placed at unique clusters of codons on the DNA. This procedure rigorously establishes the proper phasing of the DNA throughout the entire length of the structural gene, and the protein sequence is thereby accurately read from the DNA sequence. This approach is being used to determine the amino acid sequence of EScherichia coli alanine tRNA synthetase, a protein that has approximately 900 amino acids. This paper reports the sequence of the first 165 amino acids from the NH2 terminus.</protect>
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* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7005898 PubMed]

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</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{| id="E4d66d61182bdb" class=" tableEdit GO_table_reference"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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<references/>

PMID:7005898

2011-02-24T22:05:05Z

165.91.108.55: New PMID: Page!