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Fine particles in the atmosphere from soil and sand resuspension contain a variety of organic compounds from natural biogenic and anthropogenic matter. Soil and sand samples from various sites near Kuwait city were collected, sieved to retain the fine particles, and extracted with a mixture of dichloromethane and methanol. The extracts were derivatized and analyzed by gas chromatography-mass spectrometry in order to characterize the chemical compositions and sources of the organic components. The major inputs of organic compounds were from both natural biogenic and anthropogenic sources in these samples. Vegetation was the major natural source of organic compounds and included n-alkanols, n-alkanoic acids, n-alkanes, sterols and triterpenoids. Saccharides had high concentrations (31-43%) in the sand dune and seafront samples, indicating sources from decomposed vegation materials and/or the presence of viable microbiota such as bacteria and fungi. Vehicular emission products, leakage of lubricating oils, discarded plastics and emissions from cooking operations were the major anthropogenic inputs in the samples from the urban areas. This input was mainly UCM, n-alkanes, hopanes, plasticizers and cholesterol, respectively.

Three type 2C Ser/Thr phosphatases (PTCs) are negative regulators of the yeast Saccharomyces cerevisiae high-osmolarity glycerol mitogen-activated protein kinase (MAPK) pathway. Ptc2 and Ptc3 are 75% identical to each other and differ from Ptc1 in having a noncatalytic domain. Previously, we showed that Ptc1 inactivates the pathway by dephosphorylating the Hog1 MAPK; Ptc1 maintains low basal Hog1 activity and dephosphorylates Hog1 during adaptation. Here, we examined the function of Ptc2 and Ptc3. First, deletion of PTC2 and/or PTC3 together with PTP2, encoding the protein tyrosine phosphatase that inactivates Hog1, produced a strong growth defect at 37 degrees C that was dependent on HOG1, providing further evidence that PTC2 and PTC3 are negative regulators. Second, overexpression of PTC2 inhibited Hog1 activation but did not affect Hog1-Tyr phosphorylation, suggesting that Ptc2 inactivates the pathway by dephosphorylating the Hog1 activation loop phosphothreonine (pThr) residue. Indeed, in vitro studies confirmed that Ptc2 was specific for Hog1-pThr. Third, deletion of both PTC2 and PTC3 led to greater Hog1 activation upon osmotic stress than was observed in wild-type strains, although no obvious change in Hog1 inactivation during adaptation was seen. These results indicate that Ptc2 and Ptc3 differ from Ptc1 in that they limit maximal Hog1 activity. The function of the Ptc2 noncatalytic domain was also examined. Deletion of this domain decreased V(max) by 1.6-fold and increased K(m) by 2-fold. Thus Ptc2 requires an additional amino acid sequence beyond the catalytic domain defined for PTCs for full activity.

Six L-arabinose transport-deficient mutants of Salmonella typhimurium LT2 were isolated on the basis of their inability to ferment low concentrations of L-arabinose. The mutations were localized between serA and lys on the S. typhimurium genetic map and assigned to the araE locus. An araE-lac fusion strain was constructed and used to determine that the direction of araE transcription was counterclockwise on the S. typhimurium genetic map. beta-Galactosidase activity was induced by L-arabinose in the araE-lac fusion strain, suggesting that araE expression is controlled at the level of transcription.

A total of 28 L-rhamnose-negative mutants in Salmonella typhimurium LT2 were all linked by P22 transduction and were classified into five groups on the basis of genetic and biochemical experiments. Deletion mapping showed that the gene order was rhaD rhaA rhaB rhaC rhaT . rhaA mutants lacked an inducible L-rhamnose isomerase, rhaB mutants lacked an inducible L- rhamnulokinase , and rhaD mutants were probably defective in L- rhamnulose -1-phosphate aldolase. Mutants that were unable to accumulate L-[14C]rhamnose but could grow on 1% L-rhamnose were designated rhaT to indicate a defect in L-rhamnose transport. Genetic evidence supports the hypothesis that the rhaC gene is a positive regulator of rha gene expression. (i) Pleiotropically negative mutants in the rhaC gene were isolated at a high frequency. (ii) Mutants containing an insertion or deletion within the rhaC gene had a pleiotropically negative phenotype. (iii) Complementation tests indicated that rhaC + was dominant to rhaC -. (iv) Rha+ revertants of deletion and Tn10 insertion mutations in the rhaC gene were isolated.