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Biological messiness relates to infidelity, heterogeneity, stochastic noise and variation—both genetic and phenotypic—at all levels, from single proteins to organisms. Messiness comes from the complexity and evolutionary history of biological systems and from the high cost of accuracy. For better or for worse, messiness is inherent to biology. It also provides the raw material for physiological and evolutionary adaptations to new challenges.
Enzymatic conversion of adenosine to inosine is an RNA editing mechanism for post-transcriptional diversification of mRNA. A new chemical tagging–reverse transcription method leads to the identification of new A-to-I RNA editing sites in the human genome.
Secretion of strigolactone from plant roots mediates mutualistic fungal interactions but also facilitates parasitic plant invasion. A screen in Arabidopsis thaliana has identified compounds that perturb strigolactone levels and link this hormone to light signaling pathways in host plants.
Many natural products are decorated with oxygenated nitrogens, but enzymes capable of forming a stable nitroso species have been elusive. A new study reports the identification of a copper-containing C-nitrososynthase that tightly controls the oxidation state of an aromatic amine to yield the natural product 4-hydroxy-3-nitrosobenzamide.
Manipulation of stem cells is an important therapeutic goal that has proven difficult to achieve. A recent report describes a novel in vivo small-molecule screen and identifies a modulator of mammalian neurogenesis that partially reverses age-related declines in cognition.
Many nuclear and cytoplasmic proteins are post-translationally modified by both O-GlcNAc and phosphate, but determining whether a single copy of a protein bears multiple modifications remains a challenge. A new analytic approach reveals a surprising correlation between phosphorylation and the O-GlcNAc modification.
Subterranean termite colonies are founded by a single king and queen. However, the king generally outlives the queen, and an optimal number of secondary termite queens must be produced to meet the reproductive needs of the colony. A recent study explains the chemical basis of this biological process.
The multiple lysines that can link ubiquitin chains have created challenges in studying these important biopolymers. The ribosomal incorporation of a protected lysine analog now allows the specific construction of native K6- and K29-linked diubiquitin chains, enabling structural analysis and deubiquitinase profiling.
Iron-sulfur clusters are essential components of many proteins and are assembled in a hierarchical pathway. Tah18 is a diflavin reductase that transfers electrons to the [2Fe-2S] cluster of Dre2 in an early step of iron-sulfur cluster biogenesis in the cytoplasm of eukaryotes.
Structure-specific flap endonuclease 1 (FEN1) is known to interact with multiple nuclear proteins involved in DNA metabolism. Arginine methylation in FEN1 blocks phosphorylation of a nearby serine and enhances FEN1 binding to PCNA, which serves to channel FEN1 toward DNA replication and repair pathways.
Polymerase exclusion of ribonucleotides during DNA replication is imperfect. New data indicate that DNA polymerase ϵ incorporates into DNA ribonucleotides that are repaired by an RNase H2–dependent process and that defective repair results in replicative stress and genome instability.