Tracing the evolution of brain and behavior using two related species of whiptail lizards: Cnemidophorus uniparens and Cnemidophorus inornatus

Cnemidophorus whiptail lizards offer a unique opportunity to study behavioral and neural evolution because unlike most genera, ancestral and descendant species are still extant, and comparisons between species provide a window into correlated changes in biological organization through speciation. This review focuses on the all-female or parthenogenetic species Cnemidophorus uniparens (descendant species), which evolved through several hybridization events involving the sexually reproducing species Cnemidophorus inornatus (ancestral species). Data compiled over more than 2 decades include behavioral, endocrine, and neural differences between these two related species of whiptail lizards. For example, unlike females of the ancestral species, individuals of the descendant species display male-like mounting behavior (pseudocopulatory behavior) after ovulation. Pseudocopulatory behavior in the parthenogen is triggered by the progesterone surge after ovulation, and the behavioral capacity to respond to progesterone appears to be an ancestral trait that was inherited from C. inornatus males through the hybridization events. Interestingly, the regulation of sex steroid hormone receptor mRNA in brain areas critical for the expression of sociosexual behaviors differs between females of the two species and suggests that evolutionary changes in the regulation of gene expression could be a proximate mechanism that underlies the evolution of a novel social behavior in the parthenogen. Finally, because the sexual species is diploid, whereas the parthenogen is triploid, differences between the species could directly assess the effect of ploidy. The behavioral and neuroendocrinological data are pertinent for considering this possibility.     

Kinetic resolution of a conformational transition and the ATP hydrolysis step using relaxation methods with a Dictyostelium myosin II mutant containing a single tryptophan residue

The fluorescence emission intensity from a conserved tryptophan residue (W501) located in the relay loop (F466 to L516) of the Dicytostelium discoideum myosin II motor domain is sensitive to ATP binding and hydrolysis. The initial binding process is accompanied by a small quench in fluorescence, and this is followed by a large enhancement that appears coincident with the hydrolysis step. Using temperature and pressure jump methods, we show that the enhancement process is kinetically distinct from but coupled to the hydrolysis step. The fluorescence enhancement corresponds to the open-closed transition (k(obs) approximately 1000 s(-1) at 20 degrees C). From the overall steady-state fluorescence signal and the presence or absence of a relaxation transient, we conclude that the ADP state is largely in the open state, while the ADP.AlF(4) state is largely closed. At 20 degrees C the open-closed equilibria for the AMP.PNP and ADP.BeF(x) complexes are close to unity and are readily perturbed by temperature and pressure. In the case of ATP, the equilibrium of this step slightly favors the open state, but coupling to the subsequent hydrolysis step gives rise to a predominantly closed state in the steady state. Pressure jump during steady-state ATP turnover reveals the distinct transients for the rapid open-closed transition and the slower hydrolysis step.     

A cysteine-free firefly luciferase retains luminescence activity

A mutant of Photinus pyralis luciferase in which all four native cysteine residues are converted to serines retains about 10% of wild-type activity. This mutant should prove useful as a starting point for the introduction of biophysical probes of conformational changes associated with enzyme function. The activities of the cysteine-free mutant and others in which two or three cysteines are converted to serines suggest, however, that small chemical changes can have substantial and interdependent effects on bioluminescence. The introduction of probes should therefore be approached cautiously.     

The Systematics and Reproductive Biology of the Galeus arae Subspecific Complex (Chondrichthyes: Scyliorhinidae)

Galeus arae is currently classified as a complex of three subspecies (Galeus arae arae, Galeus arae antillensis, and Galeus arae cadenati). Morphometric and meristic analyses, size at maturity, and variation in color patterns, support the recognition of these taxa as distinct species. All species have well-developed nidamental glands and are oviparous. Galeus arae comprises two geographically disjunct populations that are not distinguishable by the characters we examined. A northern population occurs along the east and Gulf coasts of North America from South Carolina to the Mississippi delta, and the northern coast of Cuba to the north-eastern tip of the Yucatan. A southern population occurs along the Caribbean coasts of Honduras, Nicaragua, and Costa Rica, and some neighboring islands. Galeus antillensis occurs on the northern coasts of Hispaniola and Puerto Rico, and off many of the Leeward Islands. Galeus cadenati occurs off the Caribbean coasts of Panama and Colombia. Distributional data suggest that the three species are distributed allopatrically.     

Histamine H2 receptors on foetal-bovine articular chondrocytes.

The dose-response curve of histamine-induced cyclic AMP elevation in monolayer cultures of primary foetal-bovine articular chondrocytes was displaced to the right by cimetidine. In addition, H2 but not H1 antagonists prevented the histamine-induced cyclic AMP elevation, suggesting histamine activates chondrocyte adenylate cyclase through an H2 receptor.