PubMed · 12110752
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
John A Robertson. 2002-07-11. Ooplasmic transfer.. https://doi.org/10.1056/nejm200207113470220
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Leaves regulate gas exchange through control of stomata in the epidermis. Stomatal aperture increases when the flanking guard cells accumulate K+ or other osmolytes. K+ accumulation is stoichiometric with H+ extrusion, which is compensated for by phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31)-mediated malate synthesis. Plant PEPCs are regulated allosterically and by phosphorylation. Aspects of the signal-transduction network that control the PEPC phosphorylation state in guard cells are reported here. Guard cells were preloaded with [32P]orthophosphate (32Pi); then stomata were incubated with fusicoccin (FC), which activates the guard-cell plasma membrane H+-ATPase. [32P]PEPC was assessed by immunoprecipitation, electrophoresis, immunoblotting, and autoradiography. In -FC controls, stomatal size, guard-cell malate, and [32P]PEPC were low; maximum values for these parameters were observed in the presence of FC after a 90-min incubation and persisted for an additional 90 min. This high steady-state phosphorylation status resulted from continuous phosphorylation and dephosphorylation, even after the malate-accumulation phase. PEPC phosphorylation was diminished by approximately 80% when K+ uptake was associated with Cl- uptake and was essentially abolished when stomatal opening was sucrose--rather than K+--dependent. Finally, alkalinization by NH4+ in the presence of K+ did not cause PEPC phosphorylation (as it does in C4 plants). As discussed, a role for cytoplasmic protons cannot be completely excluded by this result. In summary, activation of the plasma membrane H+-ATPase was essential, but not sufficient, to cause phosphorylation of guard-cell PEPC. Network components downstream of the H+-ATPase influence the phosphorylation state of this PEPC isoform.
BACKGROUND: Y14 is an RNA binding protein which is part of a multiprotein complex, the exon-exon junction complex (EJC), that assembles on the exon-exon junctions of mRNAs produced by splicing. The position-specific binding of Y14 persists on mRNAs after their export to the cytoplasm. Thus, Y14, together with its interacting proteins, has the capacity to communicate to the cytoplasm the processing history of the mRNA, including the position of the removed introns, information that is likely to be important for defining premature termination codons. How Y14 and other components of the EJC are removed from mRNAs into the cytoplasm has not been determined. RESULTS: We show that Y14 but not another EJC component, Aly/REF, is present in polysome profile fractions containing one ribosome per mRNA. Using reporter constructs in an in vitro splicing/translation-coupled system, we show that Y14 remains associated with untranslated mRNAs but is removed from translationally active mRNAs. Importantly, mRNAs whose translation in vivo is prevented by the presence of strong secondary 5' UTR structure retain Y14 in the cytoplasm. CONCLUSIONS: These findings indicate that Y14 remains associated with mRNAs in the cytoplasm until they are translated, and translation is required to remove Y14 from mRNAs. Thus, the process of translation removes the splicing-dependent EJC protein imprints, which most likely function in the surveillance of mRNAs to define premature termination codons and possibly also in modulating the translation activity of cytoplasmic mRNAs.
To reduce the risk of foodborne illness, many fermented and minimally processed foods rely on the "hurdle effect", i.e. a combination of two or more inhibitory agents being more inhibitory than any of the agents alone. However, we have observed that such a combination of agents is not always more inhibitory to foodborne pathogens than one alone. In this paper, we show that a combination of NaCl and acid pH is less effective than acid pH alone in reducing the numbers of Escherichia coli O157:H45. The presence of sodium chloride reduces the bacteriocidal effect of lactic acid on logarithmically growing cells of E. coli O157:H45. with approximately 10(3)-fold more survivors at pH(o) 4.2 when 4% NaCl was added to the medium. A similar protective effect was also seen with other organic acidulants and E. coli strains. The cytoplasmic pH (pH(i)) of cells in medium at pH 4.2 containing added salt was 5.8 which was 0.56 units higher than that of cells in the same medium without added salt. When the pH(i) of cells in medium without added salt was adjusted to the same value (5.8) by adding KOH, the rate of survival was also considerably greater than that of cells in medium without added salt. These data suggest that E. coli can use NaCl to counteract acidification of its cytoplasm by organic acids, and in addition, that combinations of antimicrobial agents cannot always be relied upon to achieve additive antimicrobial effects.