The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p.

In yeast, two aminoacyl-tRNA synthetases, MetRS and GluRS, are associated with Arc1p. We have studied the mechanism of this complex formation and found that the non-catalytic N-terminally appended domains of MetRS and GluRS are necessary and sufficient for binding to Arc1p. Similarly, it is the N-terminal domain of Arc1p that contains distinct but overlapping binding sites for MetRS and GluRS. Localization of Arc1p, MetRS and GluRS in living cells using green fluorescent protein showed that these three proteins are cytoplasmic and largely excluded from the nucleus. However, when their assembly into a complex is inhibited, significant amounts of MetRS, GluRS and Arc1p can enter the nucleus. We suggest that the organization of aminoacyl-tRNA synthetases into a multimeric complex not only affects catalysis, but is also a means of segregating the tRNA- aminoacylation machinery mainly to the cytoplasmic compartment.     

The Minds of the West: Ethnocultural Evolution in the Rural Middle West, 1830-1917

The Minds of the West: Ethnocultural Evolution in the Rural Middle West, 1830-1917. Jon Gjerde. Chapel Hill: University of North Carolina Press, 1997. 426 pp.     

A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1.

NSP1 is a nuclear pore protein (nucleoporin) essential for cell growth. To identify the components that functionally interact with NSP1 in the living cell, we developed a genetic screen for mutants that are lethal in a genetic background of mutated, but not wild type NSP1. Fourteen synthetic lethal mutants were obtained, belonging to at least four different complementation groups. The genes of two complementation groups, NSP116 and NSP49, were cloned. Like the previously described nucleoporins, these genes encode proteins with many repeat sequences. NSP116 and NSP49, however, contain a new repetitive sequence motif 'GLFG', which classifies them as a subclass of nucleoporins. NSP116 and NSP49, tagged with the IgG binding domain of protein A and expressed in yeast, are located at the nuclear envelope. These data provide in vivo evidence that distinct subclasses of nucleoporins physically interact or share overlapping function in nuclear pore complexes.     

Mating behaviour in the endangered Sonoran topminnow: speciation in action

Two species of the endangered Sonoran topminnow, Poeciliopsis occidentalis and P. sonoriensis, occur in two isolated drainage systems in southeast Arizona, U.S.A., and are allopatric throughout their range. Although these two taxa are morphologically very similar, and have been previously described as the same species or subspecies, several molecular studies have since indicated that they differ more than their morphology suggests. To determine whether the behaviours of the two species function as premating barriers to reproduction, we investigated their mating preferences and behavioural patterns in a laboratory setting. Results from no-choice mating observations showed that the mating behaviours of the two species differ. Observations conducted during multiple-choice mating trials provided evidence of assortative mating, suggesting an early stage of premating reproductive isolation.