EcoliWiki - User contributions [en]

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'''Charlionet, R, Sesboue, R, Vercaigne, D and Martin, JP''' (1978) A new approach to the isolation of human alpha-1-antitrypsin: the immuno-electroelution. ''Immunochemistry'' '''15''':145-8
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!align=left |Abstract
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No abstract in PubMed
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=305887 PubMed]

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!align=left |Keywords
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Antigen-Antibody Complex; Electrophoresis, Polyacrylamide Gel; Humans; Immunoelectrophoresis/methods; alpha 1-Antitrypsin/isolation & purification

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PMID:305887

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'''Winney, RJ, Gilmour, HM and Matthews, JD''' (1976) Prednisolone in giant hypertrophic gastritis (Menetrier's disease). ''Am J Dig Dis'' '''21''':337-9
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!align=left |Abstract
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No abstract in PubMed
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=5887 PubMed]

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!align=left |Keywords
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Aged; Bronchitis/complications; Colitis, Ulcerative/complications; Edema/drug therapy; Gastritis/drug therapy; Gastritis/pathology; Humans; Hypertrophy/drug therapy; Male; Prednisolone/therapeutic use; Protein-Losing Enteropathies/drug therapy; Serum Albumin/deficiency; Stomach/pathology; Sulfasalazine/therapeutic use

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<protect>
 '''Lupker, JH, Verschoor, GJ, de Rooij, FW, Rörsch, A and Bosch, L''' (1974) An Escherichia coli mutant with an altered elongation factor Tu.''Proc. Natl. Acad. Sci. U.S.A.'' '''71''':460-3

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|{{TableHeadingColor}} |'''Abstract''' || <protect>A thermosensitive mutant of Escherichia coli has been isolated that is unable to replicate the bacteriophage MS2 at 42 degrees but permits phage production at 37 degrees . Thermal inactivation studies of the supernatant enzymes show that this mutant contains a factor essential for the polymerization of phenylalanine from phenylalanyl-tRNA that at 50 degrees is more rapidly inactivated than the corresponding wild-type factor. The elongation factor Tu (EF-Tu) was isolated and purified to apparent homogeneity as the EF-Tu.GDP complex, both from mutant and wild-type cells. Addition of purified wild-type EF-Tu.GDP to reaction mixtures fully restored the activity of thermally inactivated mutant supernatants. These experiments excluded EF-Ts as the thermolabile factor involved. Similar inactivation studies, dealing with the purified factors and performed in reaction mixtures that were not supplemented with GDP, revealed that the half-life of mutant EF-Tu.GDP at 50 degrees was 1.5 min, that of the wild-type factor 6 min. Addition of GDP (10muM) to the medium reduced the inactivation rate of both wild-type and mutant factor and also the difference in inactivation kinetics. Besides the altered elongation factor Tu, the mutant skill contains a second mutation affecting the glutaminyl-tRNA synthetase.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4592692 PubMed]

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{| id="L4be9c05ad5c6f" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:4592692

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<protect>
 '''Huisman, O, Errada, PR, Signon, L and Kleckner, N''' (1989) Mutational analysis of IS10's outside end.''EMBO J.'' '''8''':2101-9

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|{{TableHeadingColor}} |'''Abstract''' || <protect>We present the genetic analysis of a large number of mutations in the outside end of insertion sequence IS10. (i) The terminal inverted repeat sequence is probably the primary site of transposase binding. Mutations in this region fall into phenotypic classes which correspond to their map locations, suggesting that this region may consist of several distinct functional segments. Similarities between the organization of IS10's inverted repeat and those of other transposable elements are discussed. (ii) Base pairs 23-42 include a consensus binding sequence for one of the IS10 transposition host factors, IHF. The phenotypes of mutations in this region suggest that IHF is the major host factor for outside-end transposition activity in vivo and that base pairs throughout this region are important for the IHF interaction. (iii) Mutations in bp 43-61 do not affect outside-end transposition activity but do affect, in expected ways, previously identified determinants involved in expression and regulation of transposase. (iv) Some mutations in bp 23-42 also affect transposase expression; the possibility that IHF negatively regulates transcription initiation is discussed.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2551675 PubMed]

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{| id="T4be9bed309af0" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.171997.T4be9bed309af0&page=171997&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:2551675

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 '''Gamas, P, Galas, D and Chandler, M''' DNA sequence at the end of IS1 required for transposition.''Nature'' '''317''':458-60

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The insertion sequence IS1 belongs to a class of bacterial transposable genetic elements that can form compound transposons in which two copies of IS1 flank an otherwise non-transposable segment of DNA. IS1 differs from other known elements of this class (such as IS10, IS50 and IS903) in several respects. It is one of the smallest known insertion elements, exhibits a relatively complex array of open reading frames, is present in the chromosomes of various Enterobacteria, in some cases in many copies, and its insertion can result in the duplication of either 8 or 9 base pairs (bp) in the target DNA. Furthermore, although, like other members of the compound class, it seems to undergo direct transposition, IS1 also promotes replicon fusion (co-integrate formation) at a relatively high frequency. Like all other elements studied to date, the integrity of the extremities of IS1 are essential for efficient transposition. We have constructed a test system to determine the minimal DNA sequences at the extremities of IS1 required for transposition. Sequential deletions of the end sequences reveal that 21-25 bp of an isolated extremity are sufficient for transposition. A specific sequence 13-23 bp from the ends, defining the edge of the minimal sequence, is implicated as an essential site. The sites, symmetrically arrayed at both ends of IS1, correspond to the apparent consensus sequence of the known binding sites for the Escherichia coli DNA-binding protein (called integration host factor or IHF) which is required for the site-specific recombination that leads to integration of bacteriophage lambda into the bacterial genome. The sites at the ends of IS1 may thus bind a host protein, such as JHF or a related protein, that is involved in regulating the transposition apparatus.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2995832 PubMed]

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{| id="Z4be9beca503c7" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:2995832

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 '''Ohtsubo, E, Zenilman, M, Ohtsubo, H, McCormick, M, Machida, C and Machida, Y''' (1981) Mechanism of insertion and cointegration mediated by IS1 and Tn3.''Cold Spring Harb. Symp. Quant. Biol.'' '''45 Pt 1''':283-95

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|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6271477 PubMed]

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{| id="E4be9bebd46811" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.171995.E4be9bebd46811&page=171995&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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<protect>
 '''Campbell, A, Starlinger, P, Berg, DE, Botstein, D, Lederberg, EM, Novick, RP and Szybalski, W''' (1979) Nomenclature of transposable elements in prokaryotes.''Plasmid'' '''2''':466-73

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|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=384423 PubMed]

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{| id="V4be9beaf4ebe6" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:384423

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 '''Swinger, KK and Rice, PA''' (2004) IHF and HU: flexible architects of bent DNA.''Curr. Opin. Struct. Biol.'' '''14''':28-35

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The energetic cost of bending short segments of DNA is very high. This bending is critical for the packaging of DNA and is exploited to regulate many cellular processes. In prokaryotes, IHF and HU are key architectural proteins present at high concentrations. New protein-DNA co-crystal structures, and the adaptation of advanced biophysical and biochemical techniques have led to an improved understanding of how these proteins interact with DNA. These techniques include time-resolved synchrotron X-ray footprinting, differential scanning calorimetry, isothermal titration calorimetry and single-molecule experiments.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15102446 PubMed]
Online version:[http://dx.doi.org/10.1016/j.sbi.2003.12.003 10.1016/j.sbi.2003.12.003]
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{| id="H4be9be8c10ddb" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:15102446

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<protect>
 '''Feiss, M, Frackman, S and Sippy, J''' (1985) Essential interaction between lambdoid phage 21 terminase and the Escherichia coli integrative host factor.''J. Mol. Biol.'' '''183''':239-46

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|{{TableHeadingColor}} |'''Abstract''' || <protect>Lambdoid phage 21 requires the Escherichia coli integrative host factor (IHF) for growth. lambda-21 hybrids that have 21 DNA packaging specificity also require IHF. IHF-independent (her) mutants have been isolated. her mutations map in the amino-terminal half of the 21 1 gene. The 1 gene encodes the small subunit of the 21 terminase, and the amino-terminal half of the 1 polypeptide is a functional domain for specifically binding 21 DNA. Hence changes in the DNA-binding domain of terminase, her mutations, render 21 terminase able to function in the absence of IHF. Three of four her mutations studied are trans-dominant. An in vitro system was used to show that packaging of 21 DNA is IHF-dependent. IHF is directly required during the early, terminase-dependent steps of assembly. It is concluded that IHF is a host factor required for function of the 21 terminase. It is proposed, in analogy to the role of IHF in lambda integration, that IHF facilitates proper binding of 21 terminase to phage DNA. Consistent with this proposal, possible IHF-binding sites are present in the 21 cohesive end site.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2989543 PubMed]

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{| id="T4be9be81b852f" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.171992.T4be9be81b852f&page=171992&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:2989543

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PMID:2984205

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<protect>
 '''Leong, JM, Nunes-Düby, S, Lesser, CF, Youderian, P, Susskind, MM and Landy, A''' (1985) The phi 80 and P22 attachment sites. Primary structure and interaction with Escherichia coli integration host factor.''J. Biol. Chem.'' '''260''':4468-77

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|{{TableHeadingColor}} |'''Abstract''' || <protect>Although the lambdoid bacteriophage phi 80 and P22 possess site-specific recombination systems analogous to bacteriophage lambda, they have different attachment (att) site specificities. We have identified and determined the nucleotide sequences of the att sites of phi 80 and P22 and have examined the interaction of these sites with purified Escherichia coli integration host factor (IHF). The sizes of the homologous core regions of the att sites vary greatly: P22 has a 46-base pair core, while phi 80 and lambda have 17- and 15-base pair cores, respectively. The core sequences of the three phage show no significant homology, although dispersed regions of homology in arm sequences indicate that the three phage att sites are related. All three att sites have a high A + T composition, and restriction fragments carrying these sites migrate anomalously upon polyacrylamide gel electrophoresis. IHF binds to a site to the left of the common core in the phi 80 and P22 phage att sites (attP) and to a site to the right of the core in P22 attP and attB (the bacterial att site). In the lambda system, IHF interacts with three regions on attP (designated H1, H2, and H') and none on attB (Craig N., and Nash, H.A. (1984) Cell 39, 707-716). Alignment of the IHF sites of all three phage results in a consensus sequence for IHF binding, Pyr-AANNNNTTGATAT. Among the three phage, the number of IHF sites differs; however, the location and orientation of the binding sites in relation to the respective core regions are well conserved. An IHF site analogous to lambda H2 is present in both phi 80 and P22 attP, while a site analogous to lambda H' is present in P22 attP. This conservation suggests that IHF plays a very similar role in the site-specific recombination pathways of all three phage, and that the flanking arm sequences are necessary for phi 80 and P22 attP function, as is the case for lambda attP function. These structural similarities presumably reflect a conservation of the mechanism of site-specific recombination for the three phage.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2984205 PubMed]

|}
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{| id="E4be9be7a62634" class=" tableEdit GO_table_reference"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.171991.E4be9be7a62634&page=171991&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:2984205

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<protect>
 '''Nash, HA and Robertson, CA''' (1981) Purification and properties of the Escherichia coli protein factor required for lambda integrative recombination.''J. Biol. Chem.'' '''256''':9246-53

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|{{TableHeadingColor}} |'''Abstract''' || <protect>A purified preparation of the Escherichia coli integration host factor (IHF) displays two polypeptides of apparent molecular weight 11,000 and 9,500 when analyzed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Under nondenaturing conditions, IHF appears to exist as a 1:1 complex of these two polypeptides. Integrative recombination takes place in vitro when purified IHF and purified Int, a product of a bacteriophage lambda gene, are the only proteins added to reaction mixtures. No recombination is detected in the absence of either protein. The characteristics of the recombination reaction carried out by these two purified proteins are described. Purified IHF binds to DNA; in the presence of Int, a ternary complex is formed at one of the specific recombination sites. IHF hs no detectable endonuclease or topoisomerase activity. Several possibilities for the role of IHF in recombination are considered.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6267068 PubMed]

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{| id="A4be9be73aea80" 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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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.171990.A4be9be73aea80&page=171990&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:6267068

2010-05-11T20:30:43Z

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