Precise biostratigraphic constraints on the age of the Tal Group are restricted to (1) a basal level correlative with the Anabarites trisulcatus–Protohertzina anabarica Assemblage Zone of southwest China, (2) a level near the boundary of the lower and upper parts of the Tal Group correlative with the early Tsanglangpuan Stage (Drepanuroides Zone), and (3) an interval low in the upper part of the Tal Group correlative with later in the Tsanglangpuan Stage (Palaeolenus Zone). These correlations are based on small shelly fossil and trilobite taxa. Other chronostratigraphic constraints include the marked negative δ13C isotopic excursion coincident with the transition from the Krol Group to the Tal Group. This excursion is used as a proxy for the Precambrian–Cambrian boundary in several sections worldwide and, if applied to the Lesser Himalaya, indicates that the boundary is at or just above the base of the Tal Group. The upper parts of the Tal Group may be of middle or late Cambrian age and might form proximal equivalents of sections in the Zanskar–Spiti region of the Tethyan Himalaya. Both faunal content and lithological succession are comparable to southwest China, furthering recent arguments for close geographic proximity between the Himalaya and the Yangtze block during late Neoproterozoic and early Cambrian time. Trilobites from the uppermost parts of the Sankholi Formation from the Nigali Dhar syncline are described and referred to three taxa, one of which, Drepanopyge gopeni, is a new species. They are the oldest trilobites yet described from the Himalaya.
These results indicate that A. baumannii causes severe intraocular inflammation and retinal damage. Furthermore, neutrophils play an important role in the pathogenesis of A. baumannii endophthalmitis.
Genes capable of 4-chlorobiphenyl (4-CBP) degradation were cloned from 4-CBP-degrading Pseudomonas putida OU83 by using a genomic library which was constructed in the broad-host-range cosmid vector pCP13. P. putida AC812 containing chimeric cosmid-expressing enzymes involved in the 4-CBP degradation pathway were identified by detecting 3-phenylcatechol dioxygenase activity (3-PDA). Chimeric cosmid clones pOH83, pOH84, pOH85, pOH87, and pOH88 positive for 3-PDA grew in synthetic basal medium containing 4-CBP (5 mM) as a carbon source. Restriction digestion analysis of recombinant cosmids showed DNA inserts ranging from 6 to 30 kilobase pairs. Southern hybridization data revealed that the cloned DNA inserts originated from strain OU83. Gas chromatography-mass spectrometry analysis of the metabolites of P. putida AC812(pOH88) incubated with 4-CBP and 4'-chloro-3-phenylcatechol showed the formation of 4-chlorobenzoic acid and benzoic acid. These results demonstrate that the cloned DNA fragments contain genes encoding for chlorobiphenyl dioxygenase (cbpA), dihydrodiol dehydrogenase (cbpB), 4'-chloro-3-phenylcatechol dioxygenase (cbpC), a meta-cleavage compound (a chloro derivative of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate) hydrolase (cbpD), and a new dechlorinating activity (dcpE). The location of the cbpC gene specifying 3-PDA was determined by subcloning an EcoRI DNA fragment (9.8 kilobase pairs) of pOH88 in plasmid vector pUC19. The cloned gene encoding 3-PDA was expressed in Escherichia coli HB101 and had substrate specificity only for 3-phenylcatechol and 4'-chloro-3-phenylcatechol.
Consultants differed markedly in their admitting decisions about identical patients. Objective outcome prediction models might improve equity in ICU bed use for patients with COPD.
Genes encoding 3-phenylcatechol dioxygenases were cloned from the chlorobiphenyl-degrading Pseudomonas putida strain OU83, using broad-host-range cosmid vector pCP13. Restriction enzyme analysis of DNA from 2,3-dioxygenase-positive chimeric cosmids showed DNA inserts ranging in size from 6.0 to 30 kilobases. The origin of the DNA insert in hybrid clones was established by using 32P-labeled hybrid clones (pOH101 and pOH810). A 2.3-kilobase HindlIl fragment was common to two clones. The 2,3-dioxygenase from the parent P. putida strain, OU83, and the recombinant clones (pOH101 and pOH8101) showed similar characteristics as determined by isoelectric focusing and polyacrylamide gel electrophoresis. The 2,3-dioxygenase from the Escherichia coli recombinant cosmid showed a pl of 5.0, a Km of 14 ,uM, and broad substrate activity with catechol, 4-chlorocatechol, 4-methylcatechol, and 2,3-dihydroxybiphenyl.
Genes of Pseudomonas putida strains that are capable of degrading polychlorinated biphenyls were cloned in the plasmid vector pUC19. The resultant hybrid plasmid, pAW6194, contained cbpABCD genes on a 9.0-kb DNA fragment that was necessary for the catabolism of polychlorinated biphenyls. These genes were further subcloned on an 8.0-kb HindIlI fragment of pAW540. Degradation of 3-chlorobiphenyl, 2,4-dichlorobiphenyl, and 2,4,5-trichlorobiphenyl into a chloro derivative of benzoic acid was found in Escherichia coli harboring chimeric plasmid pAW540. Expression of cbpA (biphenyl dioxygenase, 6.2 U/mg of protein) and cbpC (3-phenylcatechol dioxygenase, 611.00 U/mg of protein) genes was also found in E. coli containing the hybrid plasmid pAW540. These enzyme activities were up to 10-fold higher than those found in P. putida OU83. These results led us to conclude that cbpABCD genes of P. putida OU83 were encoded on cloned DNA and expressed in E. coli. Whether the expression of cbpABCD genes of P. putida OU83 was driven by its own promoters located on the cloned DNA or by the lacZ promoter of pUCl9 was examined by subcloning a 8.0-kb DNA fragment encoding the cbpABCD genes, in both orientations, in the HindIlI site of the promoter probe vector pKK232-8. The resulting recombinant plasmids, pAW560 and pAW561, expressed cbpABCD genes and conferred chloramphenicol resistance only in E. coli harboring pAW560, indicating that the expression of chloramphenicol acetyltransferase is independent of cbpABCD gene expression. Physical mapping, subcloning, and deletion mutant plasmids allowed us to identify DNA regions encoding the cbpBCD genes on the 2.3-kb SalI-HindIll fragment and the cbpA gene on the 2.8-kb Sall fragment of pAW540. The locations of cbpA and cbpBCD genes were found to be 3.0 kb apart on the cloned DNA. The structural organization of the cbpABCD genes was also determined by TnS insertional inactivation of the genes.
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