Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phage P1 does not adsorb to S. typhinurium wild type cells. It does adsorb to rough derivatives including strains with mutations in the galE gene. Phage strain P1CM clr-100 can be efficiently propagated in S. typhimurium derivatives, either by induction of a lysogene, or by lytic infection. Phage P1 lysates are able to mobilize genetic markers in a generalized fashion. The transduction system is essentially identical to that in Escherichia coli, except that CaCl2 is not required for efficient adsorption. Two regions of the S. typhimurium chromosome were mapped by P1-mediated transduction. Several examples of genes linked by P1, and unlinked by P22, are presented. The relative efficiency of P1 over P22 in transduction was not determined, however. Data presented indicate unambigously that the gene order for the trp region is: his ... dad A-hem A-trp-pyrF ... pyrC but known markers in between were not used. The gene order for the cys A region was determined to be as follows: pheA ... purC-cys A-trz A-pts-dsd-aro D-purF ... his, and special mapping problems for this region are discussed.
Mol Gen Genet 1975
PMID:Transduction by phage P1CM clr-100 in Salmonella typhimurium. 110 47

The kinetics of production of transducing particles for different bacterial markers were followed by premature lysis of Salmonella typhimurium cells infected with P22 phages. The were compared for cells infected with wild type phage or with HT-mutants which show increased transduction frequencies. Measuring the sedimentation velocity of bacterial DNA of cells infected with wild type or HT-phages, it was shown that: a) there is no cutting of DNA at random; b) original fragments necessary for packaging host DNA into transducing particles cannot be smaller than 10 phage-genome lengths; c) cutting of transducing fragments leads immediately to the right length; d) there is no loss of precipitable DNA due to phage infection.
Mol Gen Genet 1975 Sep 29
PMID:Appearance of transducing particles and the fate of host DNA after infection of Salmonella typhimurium with P22-mutants with increased transducing ability (HT-mutants). 110 52

Phage P22-mutants with increased transduction ability (HT-mutants) show in comparison to wild type 22, different frequencies of contransduction for markers on two different transducing fragments of the Salmonella chromosome. The data are interpreted as indicating that host DNA to be packaged is cut by HT-mutants at sites different from those cut by wild-type phage, due to an altered specificity of the nuclease responsible for this step.
Mol Gen Genet 1976 Feb 02
PMID:Altered cotransduction frequencies exhibited by HT-mutants of Salmonella-phage P22. 125 Feb 21

The antigenicity of HIV-gag p17 and p25 proteins was analyzed using a panel of 52 monoclonal antibodies (mAb) derived from 17 independent fusion experiment protocols performed in 12 different laboratories. These mAb were tested for their capacity to bind peptides corresponding to sequences of HIV1-BRU-gag p17 and p25. Thirty-five overlapping peptides (P1 to P35) totally covering the p17 and p25 proteins were used. This study allowed us to identify four immunodominant regions inducing B cell response, two on p17 corresponding to P2 and P13 (amino acids 11-25 and 121-132, respectively) and two on p25 corresponding to P21 and P28-P29-P30 (a.a. 201-218 and 285-320 respectively). According to secondary structure predictions, peptides P2 and P21 contained hydrophilic alpha helix folded regions whereas P13 sequence presented a beta turn propensity. These regions and the P28-30 region were also predicted to be easily accessible to mAb. Several other p25-derived peptides: P15 (a.a. 142-156), P16 (a.a. 148-162), P19 (a.a. 176-192), P22 (a.a. 219-233) and P23 (a.a. 233-253) were recognized by mAb. No p17-derived peptide other than P2, P13 and P12 (a.a. 111-123) was found to react with mAb. Cross-blocking studies between mAb, suggested the existence of more than four distinct epitopic areas on p17 and eight on p25.
Mol Immunol 1992 Jun
PMID:Clonal analysis of murine B cell response to the human immunodeficiency virus type 1 (HIV1)-gag p17 and p25 antigens. 137 12

Bacteriophage P22 DNA packaging events occur in processive series on concatemeric phage DNA molecules. At the point where such series initiate, the DNA is recognized at a site called pac, and most molecular left ends are generated within six short regions called end sites, which are present in a 120 base-pair region surrounding the pac site. The bacteriophage P22 genes 2 and 3 proteins are required for successful generation of these ends and DNA packaging during progeny virion assembly. Mutants lacking the 162-amino-acid gene 3 protein replicate DNA and assemble functional procapsids. In this report we describe the nucleotide changes and DNA packaging phenotypes of a number of missense mutations of gene 3, which give the phage a higher than normal frequency of generalized transduction. In cells infected by these mutants, more packaging events initiate on the host chromosome than in wild-type infections, so the mutations are thought to affect the specificity of packaging initiation. In addition to having this phenotype, these mutations affect the process of phage DNA packaging in detectable ways. They may: (1) alter the target site specificity for packaging; (2) make target site recognition more promiscuous; (3) affect end site utilization; (4) alter the pac site; and (5) cause apparent random DNA packaging series initiation on phage DNA.
J Mol Biol 1992 Oct 20
PMID:Molecular genetic analysis of bacteriophage P22 gene 3 product, a protein involved in the initiation of headful DNA packaging. 143 88

Lysis protein T of phage T4 is required to allow the phage's lysozyme to reach the murein layer of the cell envelope and cause lysis. Using fusions of the cloned gene t with that of the Escherichia coli alkaline phosphatase or a fragment of the gene for the outer membrane protein OmpA, it was possible to identify T as an integral protein of the plasma membrane. The protein was present in the membrane as a homooligomer and was active at very low cellular concentrations. Expression of the cloned gene t was lethal without causing gross leakiness of the membrane. The functional equivalent of T in phage lambda is protein S. An amber mutant of gene S can be complemented by gene t, although neither protein R of lambda (the functional equivalent of T4 lysozyme) nor S possess any sequence similarity with their T4 counterparts. The murein-degrading enzymes (including that of phage P22) have in common a relatively small size (molecular masses of ca. 18,000) and a rather basic nature not exhibited by other E. coli cystosolic proteins. The results suggest that T acts as a pore that is specific for this type of enzyme.
Mol Gen Genet 1992 Nov
PMID:Lysis protein T of bacteriophage T4. 146

Previous studies with purified variants of the 434 repressor having different operator-binding specificities have demonstrated the interactions of a heterodimeric repressor with a hybrid operator site. The present study investigates the interactions between the 434 repressor and its operator site. The optimum 434 operator half-site is used with a P22 operator half-site to create a hybrid 434/P22 operator. We show that this hybrid operator can be efficiently bound by a heterodimeric repressor, consisting of one wild-type 434 repressor monomer and one 434 repressor monomer with the binding specificity of the P22 repressor, to bring about repression in Escherichia coli.
Mol Microbiol 1992 Feb
PMID:Efficient repression by a heterodimeric repressor in Escherichia coli. 155 50

The complex double-stranded DNA bacteriophages assemble DNA-free protein shells (procapsids) that subsequently package DNA. In the case of several double-stranded DNA bacteriophages, including P22, packaging is associated with cutting of DNA from the concatemeric molecule that results from replication. The mature intravirion P22 DNA has both non-unique (circularly permuted) ends and a length that is determined by the procapsid. In all known cases, procapsids consist of an outer coat protein, an interior scaffolding protein that assists in the assembly of the coat protein shell, and a ring of 12 identical portal protein subunits through which the DNA is presumed to enter the procapsid. To investigate the role of the portal protein in cutting permuted DNA from concatemers, we have characterized P22 portal protein mutants. The effects of several single amino acid changes in the P22 portal protein on the length of the DNA packaged, the density to which DNA is condensed within the virion, and the outer radius of the capsid have been determined. The results obtained with one mutant (NT5/1a) indicate no change (+/- 0.5%) in the radius of the capsid, but mature DNA that is 4.7% longer and a packing density that is commensurately higher than those of wild-type P22. Thus, the portal protein is part of the gauge that regulates the length and packaging density of DNA in bacteriophage P22. We argue that these findings make models for DNA packaging less likely in which the packing density is a property solely of the coat protein shell or of the DNA itself.
J Mol Biol 1992 Apr 20
PMID:Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA. 156 67

Amino acid sequences of primases and associated helicases involved in the DNA replication of eubacteria and bacteriophages T7, T3, T4, P4, and P22 were compared by computer-assisted methods. There are two types of such systems, the first one represented by distinct helicase and primase proteins (e.g., DnaB and DnaG proteins of Escherichia coli), and the second one by single polypeptides comprising both activities (gp4 of bacteriophages T7 and T3, and alpha protein of bacteriophage P4). Pronounced sequence similarity was revealed between approximately 250 amino acid residue N-terminal domains of stand-alone primases and the primase-helicase proteins of T7(T3) and P4. All these domains contain, close to their N-termini, a conserved Zn-finger pattern that may be implicated in template DNA recognition by the primases. In addition, they encompass five other conserved motifs some of which may be involved in substrate (NTP) binding. Significant similarity was also observed between the primase-associated helicases (DnaB, gp12 and P22 and gp41 of T4) and the C-terminal domain of T7(T3) gp4. On the other hand the C-terminal domain of P-alpha of P4 is related to another group of DNA and RNA helicases. Tentative phylogenetic trees generated for the primases and the associated helicases showed no grouping of the phage proteins, with the exception of the primase domains of bacteriophages T4 and P4. This may indicate a common origin for one-component primase-helicase systems. Two scenarios for the evolution of primase-helicase systems are discussed.(ABSTRACT TRUNCATED AT 250 WORDS)
J Mol Evol 1992 Apr
PMID:Organization and evolution of bacterial and bacteriophage primase-helicase systems. 156 88

We describe recJ mutants of Salmonella typhimurium. The recJ gene maps between sufD and serA (min 62) and is transcribed counterclockwise. Unlike recJ mutants of Escherichia coli, recJ strains of S. typhimurium are sensitive to irradiation with UV light. This sensitivity is equivalent to or greater that that displayed by recBCD mutant strains. The residual ability of phage P22 abc (anti-recBCD) mutants to form plaques on recBCD+ strains is eliminated in recJ hosts. Thus host RecJ function appears to substitute for the anti-RecBCD functions of phage P22 and may serve to limit RecBCD activity.
Mol Gen Genet 1992 Apr
PMID:The Salmonella typhimurium RecJ function permits growth of P22 abc phage on recBCD+ hosts. 158 16


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