Expression in Pisum and Lathyrus. Sandhya Tewari1,3, Stuart M. Brown1,2 and Brian Fristensky1 1Department of Plant Science, University of Manitoba, Winnipeg, R3T 2N2, CANADA. Current address: 2Cell Biology Department, NYU Medical Center, 550 First Avenue, New York, NY 10016, U.S.A. 3Confederation of Indian Industry, 23 Institutional Area, Lodi Road, New Delhi 110 003 INDIA Corresponding author:...

BACKGROUND NMR studies of denatured states, both fully unfolded and partially folded, give insight into the conformations and interactions formed during folding. Although the complete structural characterization of partially folded proteins is a very difficult task, the identification of structured subsets, such as hydrophobic clusters, is of value in understanding the structural organization o...

The molecular identity of the signal coupling intracellular Ca(2+) store depletion to the activation of Ca(2+) entry has long resisted exposure. Two recent studies independently implicate the STIM protein family as essential components in this coupling. These data provide new impetus to resolve how store Ca(2+) content is sensed and communicated to store-operated Ca(2+) channels at the cell sur...

The comparison of the three-dimensional shapes of protein molecules poses a complex algorithmic problem. Its solution provides biologists with computational tools to organize the rapidly growing set of thousands of known protein shapes, to identify new types of protein architecture, and to discover unexpected evolutionary relations, reaching back billions of years, between protein molecules. Pr...

We study two systems of tangle equations that arise when modeling the action of the Integrase family of proteins on DNA. These two systems— direct and inverted repeats—correspond to two different possibilities for the initial DNA sequence. We present one new class of solutions to the tangle equations. In the case of inverted repeats we prove that any solution not in these, or 2 previously known...

Targeting membrane proteins for degradation requires the sequential action of ESCRT sub-complexes ESCRT-0 to ESCRT-III. Although this machinery is generally conserved among kingdoms, plants lack the essential ESCRT-0 components. A new report closes this gap by identifying a novel protein family that substitutes for ESCRT-0 function in plants.

Over the last decade, there have been huge increases in the numbers of protein sequences and structures determined. In parallel, many methods have been developed for recognising similarities between these proteins, arising from their common evolutionary background, and for clustering such relatives into protein families. Here we review some of the protein family resources available to the biolo...