Respiratory Failure in a Neonate with Pierre Robin Syndrome -A Challenging Proposition.

Pierre Robin Syndrome is a well-known difficult airway condition. We present a case of successful management of a neonate in severe respiratory distress with diagnosed Pierre Robin syndrome, pneumonitis and in impending respiratory failure. We wish to highlight a sequence of measures instituted for the child including use of a supraglottic device Igel for immediate airway rescue when intubation was nearly impossible and mask ventilation very difficult. We sutured patient's tongue with his lip near the chin to keep the upper airway patent as an intermediate intervention and we could subsequently successfully treat the concomitant lung infection. Child could be discharged from hospital alive and healthy.

Piriformospora indica: a new biological hardening tool for micropropagated plants.

Piriformospora indica is a novel plant growth promoting root endophyte. Regenerated plantlets of tobacco subjected to two different biological hardening techniques showed 88-94% survival when inoculated with P. indica as compared to 62% survival of uninoculated controls under similar conditions. The tendency of the plantlet to overcome the stress in terms of revival capacity was maximal in the case of P. indica as compared to the control. The fungus has the potential to render protection to the micropropagated plantlets and help them escape the 'transient transplant shock'.

Piriformospora indica, a cultivable plant-growth-promoting root endophyte

Piriformospora indica (Hymenomycetes, Basidiomycota) is a newly described cultivable endophyte that colonizes roots. Inoculation with the fungus and application of fungal culture filtrate promotes plant growth and biomass production. Due to its ease of culture, this fungus provides a model organism for the study of beneficial plant-microbe interactions and a new tool for improving plant production systems.

Regulation of an Escherichia coli/mammalian chimeric carbamoyl-phosphate synthetase.

Carbamoyl-phosphate synthetase (CPSase) consists of a 120-kDa synthetase domain (CPS) that makes carbamoyl phosphate from ATP, bicarbonate, and ammonia usually produced by a separate glutaminase domain. CPS is composed of two subdomains, CPS.A and CPS.B. Although CPS.A and CPS.B have specialized functions in intact CPSase, the separately cloned subdomains can catalyze carbamoyl phosphate synthesis. This report describes the construction of a 58-kDa chimeric CPSase composed of Escherichia coli CPS.A catalytic subdomains and the mammalian regulatory subdomain. The catalytic parameters are similar to those of the E. coli enzyme, but the activity is regulated by the mammalian effectors and protein kinase A phosphorylation. The chimera has a single site that binds phosphoribosyl 5'-pyrophosphate (PRPP) with a dissociation constant of 25 microM. The dissociation constant for UTP of 0.23 mM was inferred from its effect on PRPP binding. Thus, the regulatory subdomain is an exchangeable ligand binding module that can control both CPS.A and CPS.B domains, and the pathway for allosteric signal transmission is identical in E. coli and mammalian CPSase. A deletion mutant that truncates the polypeptide within a postulated regulatory sequence is as active as the parent chimera but is insensitive to effectors. PRPP and UTP bind to the mutant, suggesting that the carboxyl half of the subdomain is essential for transmitting the allosteric signal but not for ligand binding.

Intranuclear binding of nucleoplasmin.

Many proteins--including not only structural proteins, but also enzymes, hormone receptors, and other transcription factors--accumulate to much higher nuclear than cytoplasmic concentrations. Nuclear localization sequences or signals (NLSs) within their primary structures entrain specific transport of these proteins through the nuclear pore complexes. This transport process is energy-dependent, but evidence for a true active transport mechanism is not conclusive. An alternative mechanism--facilitated transport of NLS proteins followed by their intranuclear binding--has been implicated by experiments with oil-isolated nuclei. However, there has been no agreement as to a role for binding in the in vivo nuclear accumulation of NLS-containing proteins. We demonstrate herein that a prototypical NLS protein, nucleoplasmin (Np), binds within the nucleus of the living Xenopus oocyte and that this binding accounts for its nuclear accumulation.