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1.
Phys Rev Lett ; 118(14): 142001, 2017 Apr 07.
Article in English | MEDLINE | ID: mdl-28430484

ABSTRACT

We investigate the possibility of qq^{'}b[over ¯]b[over ¯] tetraquark bound states using n_{f}=2+1 lattice QCD ensembles with pion masses ≃164, 299, and 415 MeV. Motivated by observations from heavy baryon phenomenology, we consider two lattice interpolating operators, both of which are expected to couple efficiently to tetraquark states: one with a diquark-antidiquark and one with a meson-meson structure. Using nonrelativistic QCD to simulate the bottom quarks, we study the udb[over ¯]b[over ¯], ℓsb[over ¯]b[over ¯] channels with ℓ=u, d, and find unambiguous signals for strong-interaction-stable J^{P}=1^{+} tetraquarks. These states are found to lie 189(10) and 98(7) MeV below the corresponding free two-meson thresholds.

2.
Phys Rev Lett ; 116(23): 232002, 2016 Jun 10.
Article in English | MEDLINE | ID: mdl-27341226

ABSTRACT

We report the first lattice QCD calculation of the hadronic vacuum polarization (HVP) disconnected contribution to the muon anomalous magnetic moment at physical pion mass. The calculation uses a refined noise-reduction technique that enables the control of statistical uncertainties at the desired level with modest computational effort. Measurements were performed on the 48^{3}×96 physical-pion-mass lattice generated by the RBC and UKQCD Collaborations. We find the leading-order hadronic vacuum polarization a_{µ}^{HVP(LO)disc}=-9.6(3.3)(2.3)×10^{-10}, where the first error is statistical and the second systematic.

3.
Phys Rev D Part Fields ; 53(5): 2563-2572, 1996 Mar 01.
Article in English | MEDLINE | ID: mdl-10020251
6.
Phys Rev D Part Fields ; 51(1): 132-135, 1995 Jan 01.
Article in English | MEDLINE | ID: mdl-10018278
8.
Phys Rev D Part Fields ; 44(3): 751-755, 1991 Aug 01.
Article in English | MEDLINE | ID: mdl-10013928
11.
Phys Rev Lett ; 64(2): 161-164, 1990 Jan 08.
Article in English | MEDLINE | ID: mdl-10041665
12.
Phys Rev C Nucl Phys ; 39(5): 1889-1895, 1989 May.
Article in English | MEDLINE | ID: mdl-9955412
13.
Phys Rev Lett ; 59(6): 627-629, 1987 Aug 10.
Article in English | MEDLINE | ID: mdl-10035829
14.
Phys Rev D Part Fields ; 34(5): 1372-1375, 1986 Sep 01.
Article in English | MEDLINE | ID: mdl-9957297
15.
J Virol ; 47(3): 399-405, 1983 Sep.
Article in English | MEDLINE | ID: mdl-6620460

ABSTRACT

The DNA synthesized in the nonpermissive host by the noncomplementing mutants am36 and am42 of bacteriophage phi W-14 contains about half the wild-type level of alpha-putrescinylthymine (putThy) and a correspondingly greater level of thymine. The mechanisms whereby thymine nucleotides are excluded from replicating DNA are functional in both mutants because neither of them incorporates exogenous thymidine into DNA. It is proposed that (i) in wild-type phi W-14, the conversion of hydroxymethyluracil to putThy at the polynucleotide level is sequence specific, but that to thymine is nonspecific; and (ii) in the mutants, the sequence-specific recognition is impaired so that more thymine and less putThy are formed. The thymine-rich DNA can be packaged into phage particles. In the case of am42, the phage particles are morphologically indistinguishable from and have essentially the same polypeptide composition as wild-type particles. However, the DNA molecules they contain are about 11% shorter than those in wild-type phage, am42rev4, a revertant of am42, contains DNA with about 70% of the normal level of putThy; these molecules are about 3% shorter than wild-type DNA. The properties of am42 and am42rev4 are consistent with the suggestion that putThy facilitates the very tight packing of phi W-14 DNA (Scraba et al., Virology 124:152-160, 1983). It also appears that the putThy content of phi W-14 DNA can be reduced by no more than 30% without adversely affecting the production of viable progeny; for example, the burst size of am42rev4 is about 25% of that of the wild type.


Subject(s)
Bacteriophages/physiology , DNA, Viral/metabolism , Thymine/analogs & derivatives , Bacteriophages/genetics , Base Composition , Base Sequence , DNA, Viral/analysis , Mutation , Pseudomonas , Thymine/biosynthesis , Thymine/physiology , Viral Proteins/analysis , Viral Structural Proteins
17.
J Bacteriol ; 152(3): 1022-32, 1982 Dec.
Article in English | MEDLINE | ID: mdl-6292159

ABSTRACT

The genetic organization and interrelationships between the two ribosomal protein transcription units (the L11 and L10 operons) from near 89 min on the Escherichia coli chromosome were studied by using insertional mutations generated by the kanamycin-resistant transposable element Tn5. The polar effects of Tn5 insertions on the expression of the L11, L1, L10, and L12 ribosomal protein genes and the beta RNA polymerase subunit gene were examined (i) by the level of beta-galactosidase activity generated from L10-lacZ and beta-lacZ gene fusions, (ii) by direct sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the proteins specified by plasmid ribosomal protein genes in UV-irradiated maxicells, and (iii) by urea-polyacrylamide gel electrophoresis of plasmid- and chromosome-specified L12 protein. The results confirmed the organization of these genes into two transcription units as follows: PL11, rplK (L11), rplA (L1), PL10, rplJ (L10), rplL (L12), rpoB (beta). . .; they also localized the position of the PL10 promoter within an 80-nucleotide region near the end of the L1 gene. The results also support the idea that the translational regulatory proteins for the L11 and L10 operons are L1 and L10, respectively, and that the expression of the L12 gene is closely linked to L10 gene expression.


Subject(s)
DNA Transposable Elements , DNA-Directed RNA Polymerases/genetics , Escherichia coli/genetics , Operon , Ribosomal Proteins/genetics , Bacterial Proteins/genetics , DNA, Recombinant , Escherichia coli/metabolism , Gene Expression , Gene Expression Regulation , Genes, Bacterial , Ribosomal Proteins/biosynthesis
18.
J Virol ; 43(1): 67-72, 1982 Jul.
Article in English | MEDLINE | ID: mdl-7109031

ABSTRACT

Of 42 amber mutants of bacteriophage phi W-14, 6 were defective in DNA synthesis. Three of the mutants synthesized DNA in the nonpermissive host, but were defective in post-replicational modification of the DNA. The DNA synthesized by two of these mutants, am36 and am42, contained more thymine and less alpha-putrescinylthymine than did wild-type DNA; that synthesized by the third mutant, am37, contained the normal amount of thymine, no alpha-putrescinylthymine, and hydroxymethyluracil. The properties of these mutants suggested that the presence of the normal amount of alpha-putrescinylthymine in phi W-14 DNA was essential for the production of viable progeny. Three of the mutants, am6, am35, and am45, failed to synthesize DNA in the nonpermissive host. These mutants were analogous to the DNA off mutants of T4. Nonpermissive cells infected with DNA off mutants accumulated dATP, dGTP, dCTP, and hydroxymethyl dUTP, but not dTTP or alpha-putrescinyldeoxythymidine triphosphate, confirming that both thymine and alpha-putrescinylthymidine in phi W-14 DNA are formed from hydroxymethyluracil at the polynucleotide level. The synthesis of phi W-14 DNA is unusual because (i) thymine is formed from hydroxymethyluracil at the polynucleotide level, (ii) the hypermodification forming alpha-putrescinylthymine is essential, and (iii) thymine and alpha-putrescinylthymine must be made in the correct proportions. Complementation tests showed that the mutants defined three genes involved in DNA polymerization and two genes involved in post-replicational modification.


Subject(s)
Bacteriophages/genetics , DNA, Viral/biosynthesis , Genes, Viral , Bacteriophages/metabolism , Centrifugation, Density Gradient , Genetic Complementation Test , Mutation , Pseudomonas , Uracil/metabolism
19.
Biochemistry ; 20(12): 3586-91, 1981 Jun 09.
Article in English | MEDLINE | ID: mdl-7260058

ABSTRACT

In a nonpermissive host, an amber mutant, am 37, of bacteriophage phi W-14 synthesizes deoxyribonucleic acid (DNA) of considerably greater buoyant density than the DNA synthesized by wild-type phage. The am 37 DNA lacks the hypermodified pyrimidine, alpha-putrescinylthymine (putThy). Instead, it contains a new modified base, 5-[(hydroxymethyl)-O-pyrophosphoryl]uracil (hmPPUra). Extracts of cells infected with wild-type phi W-14 convert the hmPPUra in am 37 DNA to putThy when incubated with putrescine.


Subject(s)
Bacteriophages/metabolism , DNA, Viral/biosynthesis , Pseudomonas/metabolism , Thymine/analogs & derivatives , Uracil/analogs & derivatives , Cell-Free System , DNA Replication , Kinetics , Thymine/biosynthesis , Uracil/metabolism , Virus Replication
20.
J Virol ; 34(2): 354-9, 1980 May.
Article in English | MEDLINE | ID: mdl-6445427

ABSTRACT

Host DNA synthesis stopped about 10 min after the infection of Pseudomonas acidovorans with bacteriophage phi W-14, but host DNA was not degraded to acid-soluble fragments. The synthesis of host but not of phage DNA was inhibited by 5-fluorodeoxyuridine. The nucleotide pools of infected cells did not contain dTTP, and infection resulted in the appearance of dTTPase activity. Although ornithine labeled the alpha-putrescinylthymine residues of phi W-14 DNA, ornithine-labeled nucleotides were not detected in infected cells. A new deoxynucleoside triphosphate did appear in infected cells, but it was not labeled by ornithine. It is concluded that the thymine and alpha-putrescinylthymine in phi W-14 DNA are synthesized at the polynucleotide level.


Subject(s)
Bacteriophages/metabolism , Pseudomonas/metabolism , Thymine/analogs & derivatives , Thymine/biosynthesis , Bacteriophages/growth & development , DNA, Bacterial/metabolism , DNA, Viral/biosynthesis , Floxuridine/pharmacology , Thymidine/metabolism , Thymine Nucleotides/metabolism
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