Subscribe: Nature Chemical Biology - AOP - science feeds
Preview: Nature Chemical Biology - AOP - science feeds

Nature Chemical Biology

Nature Chemical Biology is a monthly multidisciplinary journal providing an international forum for the timely publication of significant new research at the interface between chemistry and biology. Published in hard copy and online, Nature Chemical Biolo


A heme-dependent enzyme forms the nitrogen–nitrogen bond in piperazate


Molecules containing a nitrogen–nitrogen (N–N) linkage have a variety of structures and biological activities; however, no enzyme has yet been demonstrated to catalyze N–N bond formation in an organic molecule. Here we report that the heme-dependent enzyme KtzT from Kutzneria sp. 744 catalyzes N–N bond formation in the biosynthesis of piperazate, a building block for nonribosomal peptides.

Cpf1 proteins excise CRISPR RNAs from mRNA transcripts in mammalian cells


Cpf1 is a CRISPR effector protein that has greater specificity than Streptococcus pyogenes Cas9 (SpCas9) in genome-editing applications. Here we show that Lachnospiraceae bacterium (Lb) and Acidaminococus sp. (As) Cpf1 orthologs have RNase activities that can excise multiple CRISPR RNAs (crRNAs) from a single RNA polymerase II–driven RNA transcript expressed in mammalian cells. This property simplifies modification of multiple genomic targets and can be used to increase the efficiency of Cpf1-mediated editing.

Site-specific incorporation of phosphotyrosine using an expanded genetic code


Access to phosphoproteins with stoichiometric and site-specific phosphorylation status is key to understanding the role of protein phosphorylation. Here we report an efficient method to generate pure, active phosphotyrosine-containing proteins by genetically encoding a stable phosphotyrosine analog that is convertible to native phosphotyrosine. We demonstrate its general compatibility with proteins of various sizes, phosphotyrosine sites and functions, and reveal a possible role of tyrosine phosphorylation in negative regulation of ubiquitination.

Autocatalytic backbone N-methylation in a family of ribosomal peptide natural products


Peptide backbone N-methylation, as seen in cyclosporin A, has been considered to be exclusive to nonribosomal peptides. We have identified the first post-translationally modified peptide or protein harboring internal α-N-methylations through discovery of the genetic locus for the omphalotins, cyclic N-methylated peptides produced by the fungus Omphalotus olearius. We show that iterative autocatalytic activity of an N-methyltransferase fused to its peptide substrate is the signature of a new family of ribosomally encoded metabolites.