In search of planets and life around other stars

The discovery of over a dozen low-mass companions to nearby stars has intensified scientific and public interest in a longer term search for habitable planets like our own. However, the nature of the detected companions, and in particular whether they resemble Jupiter in properties and origin, remains undetermined.

Tree rings, carbon dioxide, and climatic change

Tree rings have been used in various applications to reconstruct past climates as well as to assess the effects of recent climatic and environmental change on tree growth. In this paper we briefly review two ways that tree rings provide information about climate change and CO2: (i) in determining whether recent warming during the period of instrumental observations is unusual relative to prior centuries to millennia, and thus might be related to increasing greenhouse gases; and (ii) in evaluating whether enhanced radial growth has taken place in recent decades that appears to be unexplained by climate and might instead be due to increasing atmospheric CO2 or other nutrient fertilization. It is found that a number of tree-ring studies from temperature-sensitive settings indicate unusual recent warming, although there are also exceptions at certain sites. The present tree-ring evidence for a possible CO2 fertilization effect under natural environmental conditions appears to be very limited.

Brown dwarfs: At last filling the gap between stars and planets

Until the mid-1990s a person could not point to any celestial object and say with assurance that “here is a brown dwarf.” Now dozens are known, and the study of brown dwarfs has come of age, touching upon major issues in astrophysics, including the nature of dark matter, the properties of substellar objects, and the origin of binary stars and planetary systems.

Extrasolar planets

The first known extrasolar planet in orbit around a Sun-like star was discovered in 1995. This object, as well as over two dozen subsequently detected extrasolar planets, were all identified by observing periodic variations of the Doppler shift of light emitted by the stars to which they are bound. All of these extrasolar planets are more massive than Saturn is, and most are more massive than Jupiter. All orbit closer to their stars than do the giant planets in our Solar System, and most of those that do not orbit closer to their star than Mercury is to the Sun travel on highly elliptical paths. Prevailing theories of star and planet formation, which are based on observations of the Solar System and of young stars and their environments, predict that planets should form in orbit about most single stars. However, these models require some modifications to explain the properties of the observed extrasolar planetary systems.

Chaperone rings in protein folding and degradation

Chaperone rings play a vital role in the opposing ATP-mediated processes of folding and degradation of many cellular proteins, but the mechanisms by which they assist these life and death actions are only beginning to be understood. Ring structures present an advantage to both processes, providing for compartmentalization of the substrate protein inside a central cavity in which multivalent, potentially cooperative interactions can take place between the substrate and a high local concentration of binding sites, while access of other proteins to the cavity is restricted sterically. Such restriction prevents outside interference that could lead to nonproductive fates of the substrate protein while it is present in non-native form, such as aggregation. At the step of recognition, chaperone rings recognize different motifs in their substrates, exposed hydrophobicity in the case of protein-folding chaperonins, and specific “tag” sequences in at least some cases of the proteolytic chaperones. For both folding and proteolytic complexes, ATP directs conformational changes in the chaperone rings that govern release of the bound polypeptide. In the case of chaperonins, ATP enables a released protein to pursue the native state in a sequestered hydrophilic folding chamber, and, in the case of the proteases, the released polypeptide is translocated into a degradation chamber. These divergent fates are at least partly governed by very different cooperating components that associate with the chaperone rings: that is, cochaperonin rings on one hand and proteolytic ring assemblies on the other. Here we review the structures and mechanisms of the two types of chaperone ring system.

Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases.

Most helicases studied to date have been characterized as oligomeric, but the relation between their structure and function has not been understood. The bacteriophage T7 gene 4 helicase/primase proteins act in T7 DNA replication. We have used electron microscopy, three-dimensional reconstruction, and protein crosslinking to demonstrate that both proteins form hexameric rings around single-stranded DNA. Each subunit has two lobes, so the hexamer appears to be two-tiered, with a small ring stacked on a large ring. The single-stranded DNA passes through the central hole of the hexamer, and the data exclude substantial wrapping of the DNA about or within the protein ring. Further, the hexamer binds DNA with a defined polarity as the smaller ring of the hexamer points toward the 5' end of the DNA. The similarity in three-dimensional structure of the T7 gene 4 proteins to that of the Escherichia coli RuvB helicase suggests that polar rings assembled around DNA may be a general feature of numerous hexameric helicases involved in DNA replication, transcription, recombination, and repair.