Test of charge conjugation invariance.

We report on the first determination of upper limits on the branching ratio (BR) of eta decay to pi0pi0gamma and to pi0pi0pi0gamma. Both decay modes are strictly forbidden by charge conjugation (C) invariance. Using the Crystal Ball multiphoton detector, we obtained BR(eta-->pi0pi0gamma)<5 x 10(-4) at the 90% confidence level, in support of C invariance of isoscalar electromagnetic interactions of the light quarks. We have also measured BR(eta-->pi0pi0pi0gamma)<6 x 10(-5) at the 90% confidence level, in support of C invariance of isovector electromagnetic interactions.

Dynamics of the pi(-)p-->pi(0)pi(0)n reaction for p(pi(-))<750 MeV/c.

Data are presented for the reaction pi(-)p-->pi(0)pi(0)n in the range from threshold to p(pi(-))=750 MeV/c. The systematics of the data and multipole analyses are examined for sensitivity to a f(0)(600) ("sigma") meson. A one-pion-exchange mechanism is found to be very weak, or absent. The reaction appears to become dominated by sequential pi(0) decays through the Delta(1232) resonance as the beam momentum increases, along with substantial interference effects from several competing mechanisms.

Properties of the Lambda(1670)(1-)/2 resonance.

Recently the Crystal Ball Collaboration measured precise new data for the near-threshold reaction K(-)p-->etaLambda, which is dominated by formation of the Lambda(1670)1 / 2(-). In this Letter, we present results of a unitary, multichannel analysis that incorporates the new Crystal Ball data. For our preferred fit, we obtain mass M = 1673+/-2 MeV, width Gamma = 23+/-6 MeV, and elasticity x = 0.37+/-0.07. This elasticity is significantly larger than previously recognized. Resonance parameters of our preferred fit are in striking agreement with the quark-model predictions of Koniuk and Isgur.

Determination of the quadratic slope parameter in eta-->3pi(0) decay.

We have determined the quadratic slope parameter alpha for eta-->3pi(0) to be alpha = -0.031(4) from a 99% pure sample of 10(6)eta-->3pi(0) decays produced in the reaction pi(-)p-->n(eta) close to the eta threshold using the Crystal Ball detector at the AGS. The result is four times more precise than the present world data and disagrees with current chiral perturbation theory calculations by about four standard deviations.

Measurement of pi(0)pi(0) production in the nuclear medium by pi(-) interactions at 0.408 GeV/c.

We report on an investigation of the (pi(-),pi(0)pi(0)) reaction by means of measurements of the pi(0)pi(0) invariant mass distributions from pi(-) interactions on H, D, C, Al, and Cu targets at p(pi(-)) = 0.408 GeV/c. The sharp, strong peak in the pi(+)pi(-) invariant mass near 2m(pi) reported by the CHAOS Collaboration is not seen in our pi(0)pi(0) data. However, we do observe a change in the shape of the pi(0)pi(0) invariant mass spectrum for the different targets, indicating that the pi(0)pi(0) interaction diminishes in the nuclear medium as represented by nuclei D, C, Al, and Cu, compared to hydrogen.

Novel two-component transmembrane transcription control: regulation of iron dicitrate transport in Escherichia coli K-12.

Citrate and iron have to enter only the periplasmic space in order to induce the citrate-dependent iron(III) transport system of Escherichia coli. The five transport genes fecABCDE form an operon and are transcribed from fecA to fecE. Two genes, termed fecI and fecR, that mediate induction by iron(III) dicitrate have been identified upstream of fecA. The fecI gene encodes a protein of 173 amino acids (molecular weight, 19,478); the fecR gene encodes a protein of 317 amino acids (molecular weight, 35,529). Chromosomal fecI::Mu d1 mutants were unable to grow with iron(III) dicitrate as the sole iron source and synthesized no FecA outer membrane receptor protein. Growth was restored by transformation with plasmids encoding fecI or fecI and fecR. FecA and beta-galactosidase syntheses under transcription control of the fecB gene (fecB::Mu d1) were constitutive in fecI transformants and were regulated by iron(III) dicitrate in fecI fecR transformants. The amino acid sequence of the FecI protein contains a region close to the carboxy-terminal end for which a helix-turn-helix motif is predicted, which is typical for DNA-binding regulatory proteins. The FecI protein was found in the membrane, and the FecR protein was found in the periplasmic fraction. It is proposed that the FecR protein is the sensor that recognizes iron(III) dicitrate in the periplasm. The FecI protein activates fec gene expression by binding to the fec operator region. In the absence of citrate, FecR inactivates FecI. The lack of sequence homologies to other transmembrane signaling proteins and the location of the two proteins suggest a new type of transmembrane control mechanism.

Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli.

The fec region of the Escherichia coli chromosome determines a citrate-dependent iron(III) transport system. The nucleotide sequence of fec revealed five genes, fecABCDE, which are transcribed from fecA to fecE. The fecA gene encodes a previously described outer membrane receptor protein. The fecB gene product is formed as a precursor protein with a signal peptide of 21 amino acids; the mature form, with a molecular weight of 30,815, was previously found in the periplasm. The fecB genes of E. coli B and E. coli K-12 differed in 3 nucleotides, of which 2 gave rise to conservative amino acid exchanges. The fecC and fecD genes were found to encode very hydrophobic polypeptides with molecular weights of 35,367 and 34,148, respectively, both of which are localized in the cytoplasmic membrane. The fecE product was a rather hydrophilic but cytoplasmic membrane-bound protein of Mr 28,189 and contained regions of extensive homology to ATP-binding proteins. The number, structural characteristics, and locations of the FecBCDE proteins were typical for a periplasmic-binding-protein-dependent transport system. It is proposed that after FecA- and TonB-dependent transport of iron(III) dicitrate across the outer membrane, uptake through the cytoplasmic membrane follows the binding-protein-dependent transport mechanism. FecC and FecD exhibited homologies to each other, to the N- and C-terminal halves of FhuB of the iron(III) hydroxamate transport system, and to BtuC of the vitamin B12 transport system. FecB showed some homology to FhuD, suggesting that the latter may function in the same manner as a binding protein in iron(III) hydroxamate transport. The close homology between the proteins of the two iron transport systems and of the vitamin B12 transport system indicates a common evolution for all three systems.

Genetics of the iron dicitrate transport system of Escherichia coli.

Escherichia coli B and K-12 express a citrate-dependent iron(III) transport system for which three structural genes and their arrangement and products have been determined. The fecA gene of E. coli B consists of 2,322 nucleotides and encodes a polypeptide containing a signal sequence of 33 amino acids. The cleavage site was determined by amino acid sequence analysis of the unprocessed protein and the mature protein. For the processed form a length of 741 amino acids was calculated. The mature FecA protein in the outer membrane contains at the N terminus the "TonB box," a pentapeptide, which has hitherto been found in all receptors and colicins which functionally require the TonB protein. In addition, the dyad repeat sequence GAAAATAATTCTTATTTCG is proposed to serve as the binding site of the Fur iron repressor protein. The fecB gene was mapped downstream of fecA and encodes a protein with an apparent molecular weight of 30,000. It was synthesized as a precursor, and the mature form was found in the periplasm. The fecD gene follows fecB and was related to a membrane-bound protein with an apparent molecular weight of 28,000. In Mu d1 insertion mutants upstream of fecA, the fec genes were not inducible by iron limitation and citrate, indicating a regulatory region, termed fecI, which controls fec gene expression.