Predictions of SUSY Masses in the Minimal SUSY GUT

The MSSM distinguishes itself from other GUT's by a successful prediction of many unrelated phenomena with a minimum number of parameters. Among them: a) Unification of the couplings constants; b)Unification of the masses; c) Proton decay; d) Electroweak symmetry breaking. A combined fit of the free parameters in the MSSM to these low energy constraints shows that the MSSM model can satisfy these constraints simultaneously. From the fitted parameters the masses of the as yet unobserved superpartners of the SM particles are predicted. The 2nd order QCD coupling constant is required to be between 0.108 and 0.132. It is shown that a top mass of $174\pm16$ GeV, as suggested recently by the CDF Collaboration, constrains the mixing angle between the Higgs doublets in the MSSM to: 1.2<\tb<5.5 at the 90% C.L.. The most probable value corresponds to \tb = 1.56, which leads to a stop mass below the top mass. In this case the stop production in $p\bar{p}$ collisions would contribute to the top signature. This could be an explanation for the large effective $t\bar{t}$ cross section observed by CDF.Comment: latex + eps fig IEKP-KA/94-0

Periplasmic domain of the sensor-kinase BvgS reveals a new paradigm for the Venus flytrap mechanism

Two-component sensory transduction systems control important bacterial programs. In Bordetella pertussis, expression of the virulence regulon is controlled by the unorthodox BvgAS two-component system. BvgS is the prototype of a family of sensor-kinases that harbor periplasmic domains homologous to bacterial solute-binding proteins. Although BvgAS is active under laboratory conditions, no activating signal has been identified, only negative modulators. Here we show that the second periplasmic domain of BvgS interacts with modulators and adopts a Venus flytrap (VFT) fold. X-ray crystallography reveals that the two lobes of VFT2 delimitate a ligand-binding cavity enclosing fortuitous ligands. Most substitutions of putative ligand-binding residues in the VFT2 cavity keep BvgS active, and alteration of the cavity's electrostatic potential affects responsiveness to modulation. The crystal structure of this VFT2 variant conferring constitutive kinase activity to BvgS shows a closed cavity with another nonspecific ligand. Thus, VFT2 is closed and active without a specific agonist ligand, in contrast to typical VFTs. Modulators are antagonists of VFT2 that interrupt signaling. BvgAS is active for most of the B. pertussis infectious cycle, consistent with the proposed mechanism