The model organism Tetrahymena thermopile carries two nuclei with distinct genomes: an unrearranged germline genome with five chromosomes, and a somatic genome reduced in size by a third and with 181 chromosomes.
It is technically difficult to identify transport proteins, but here a method is presented that exploits the principle that they are stabilized in detergent solution when they bind their substrate.
A previously unappreciated histone methylation pathway helps limit DNA double-strand break formation and recombination in heterochromatin during meiosis.
Multimegadalton intraflagellar transport (IFT) trains assemble by sequential recruitment of IFT subcomplexes from the cell body to the ciliary basal bodies and tubulin, the main IFT cargo, is loaded briefly before trains depart.
Cyanine fluorophores are encoded as non-canonical amino acids to produce functional proteins in cell-free translation systems and live cells for single-molecule imaging.
Building on previous work (Pless, 2013), we argue that side-chain 'flip out' is a key event in potassium channel C-type inactivation, and propose a new method for encoding multiple noncanonical amino acids and controlling protein stoichiometry.
The first genetic compelling evidence for post-meiotic DNA double-strand breaks and its relation to chromatin remodeling in haploid pronuclei is shown.
