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TABLE OF CONTENTS |
March 2016 Volume 12, Issue 3 |
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|  | Advertisement |  |  |  | Nature Insight Frontiers in Biology
This year's Frontiers in Biology Insight features Reviews on the processes that underlie metastasis, the positive influence of inflammation on tissue repair, the role of endothelial cells in organ development, growth and regeneration, the endoplasmic reticulum stress response and its contribution to disease, and antibiotic resistance. | | |
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Research Highlights | Top |
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Optogenetics: Follow the PIF | Target identification: Getting cholesterol out | Catalytic DNA: Ligating with lambda | RNA modification: Translating for growth
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News and Views | Top |
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Perspective | Top |
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Brief Communication | Top |
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Addicting diverse bacteria to a noncanonical amino acid pp138 - 140 Drew S Tack, Jared W Ellefson, Ross Thyer, Bo Wang, Jimmy Gollihar et al. doi:10.1038/nchembio.2002

Expansion of the genetic code to noncanonical amino acids (NCAAs) has been limited by the lack of evolutionary pressure for organismal dependence on the NCAA. Linking bacterial survival to an engineered β-lactamase that requires a non-natural tyrosine analog engenders diverse bacteria with a stable, expanded genetic code.
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Articles | Top |
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A two-state activation mechanism controls the histone methyltransferase Suv39h1 pp188 - 193 Manuel M Muller, Beat Fierz, Lenka Bittova, Glen Liszczak and Tom W Muir doi:10.1038/nchembio.2008

Suv39h1 is a histone methyltransferase that methylates H3K9 residues in heterochromatic regions of the genome. An approach using semisynthetic chromatin reveals a mechanism for heterochromatin spreading in which H3K9 trimethylation anchors and activates Suv39h1 for modification of proximal lysines.
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A pyridoxal phosphate-dependent enzyme that oxidizes an unactivated carbon-carbon bond pp194 - 199 Yi-Ling Du, Rahul Singh, Lona M Alkhalaf, Eugene Kuatsjah, Hai-Yan He et al. doi:10.1038/nchembio.2009

Pyridoxal 5-phosphate (PLP) is an essential coenzyme involved in diverse amino acid transformations. The discovery that Ind4 catalyzes the PLP-dependent oxidation of an unactivated carbon of L-arginine, as a part of the indolmycin biosynthetic pathway, expands the scope of reactions facilitated by PLP-dependent enzymes.
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