Monday, August 20, 2012

Nature Chemical Biology Contents: September 2012 Volume 8 Number 9, pp 738 - 805

Nature Chemical Biology

TABLE OF CONTENTS

September 2012 Volume 8, Issue 9

Research Highlights
News and Views
Brief Communications
Articles
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Research Highlights

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Regulation: Positively alarming | Virology: Cholesterol manipulation | Proteomics: Cross-talking modifications | Synthetic biology: Beta testing | Drug resistance: The stroma's contribution | Iron-sulfur clusters: MMS to the nucleus | Prodrug activation: Glutaredoxin family tree | Immunity: FetA gets fat

News and Views

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Peroxidasin: Tying the collagen-sulfilimine knot   pp740 - 741
Stephen J Weiss
doi:10.1038/nchembio.1050
Type IV collagen, a major constituent of basement membranes, contains an unusual intermolecular sulfilimine crosslink whose route of biosynthesis has remained undefined. An oxidative triad consisting of peroxidasin, H2O2 and halide is now shown to drive sulfilimine generation in vivo.

See also: Article by Bhave et al.

Glycosyltransferases: Carb loading strategy is spot on   pp741 - 742
Jeffrey C Gildersleeve
doi:10.1038/nchembio.1049
Glycosyltransferases, enzymes that catalyze glycosidic bond formation, are one of the most important but least well-characterized protein families found in nature. A new label-free, high-throughput glycan array-based strategy enables rapid profiling of tens of thousands of potential glycosyltransferase reactions.

See also: Article by Ban et al.

Membranes: First steps to rafts?   pp743 - 744
John R Silvius
doi:10.1038/nchembio.1045
Single-molecule observations reveal that lipid- and protein-based interactions jointly contribute to the interactions among glycosylphosphatidylinositol-anchored proteins in membranes. Understanding these interactions will help to refine long-evolving (and still debated) models of 'raft' domains in biological membranes.

See also: Article by Suzuki et al.

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Brief Communications

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Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection   pp745 - 747
Aaron W Puri, Petr Broz, Aimee Shen, Denise M Monack and Matthew Bogyo
doi:10.1038/nchembio.1023



AWP28, an activity-based probe for caspase-1, reveals that caspase-1 is required to bypass apoptosis for pyroptotic cell death during bacterial infection of macrophages.

Expanding the genetic code of Drosophila melanogaster    pp748 - 750
Ambra Bianco, Fiona M Townsley, Sebastian Greiss, Kathrin Lang and Jason W Chin
doi:10.1038/nchembio.1043



Genetic code expansion by ribosomal incorporation of non-natural amino acids has provided a useful approach for site-specific protein modification. This approach has now been extended to the model organism Drosophila melanogaster, permitting the introduction of non-standard amino acids into proteins within specific cell and tissue types and across developmental stages.
Chemical compounds

Articles

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AID/APOBEC deaminases disfavor modified cytosines implicated in DNA demethylation   pp751 - 758
Christopher S Nabel, Huijue Jia, Yu Ye, Li Shen, Hana L Goldschmidt, James T Stivers, Yi Zhang and Rahul M Kohli
doi:10.1038/nchembio.1042



AID/APOBEC deaminases, which convert cytosine bases to uracils in DNA and RNA, have recently been assigned a role in epigenetic regulation as components of DNA demethylation pathways. A systematic study shows that AID/APOBEC enzymes preferentially deaminate unmodified cytosine over its C5-modified forms, calling into question the plausibility of deaminase-mediated DNA demethylation pathways.

Architectural and thermodynamic principles underlying intramembrane protease function   pp759 - 768
Rosanna P Baker and Sinisa Urban
doi:10.1038/nchembio.1021



Application of a new thermal light scattering technique to quantitatively analyze nearly 150 mutants of the rhomboid intramembrane protease GlpG, coupled with thermodynamic measurements and protease assays, reveals how interactions throughout the molecule collaborate to support enzyme structure and function.

Discovery of glycosyltransferases using carbohydrate arrays and mass spectrometry   pp769 - 773
Lan Ban, Nicholas Pettit, Lei Li, Andreea D Stuparu, Li Cai, Wenlan Chen, Wanyi Guan, Weiqing Han, Peng George Wang and Milan Mrksich
doi:10.1038/nchembio.1022



Discovery of the native activity of the ~60,000 putative glycosyltransferases remains a substantial challenge. A high-throughput, label-free method drastically speeds this process, with assays of 85 enzymes, 24 acceptors and 7 donors returning functions for four new proteins.
Chemical compounds
See also: News and Views by Gildersleeve

Transient GPI-anchored protein homodimers are units for raft organization and function   pp774 - 783
Kenichi G N Suzuki, Rinshi S Kasai, Koichiro M Hirosawa, Yuri L Nemoto, Munenori Ishibashi, Yoshihiro Miwa, Takahiro K Fujiwara and Akihiro Kusumi
doi:10.1038/nchembio.1028



Single-molecule imaging reveals that GPI-anchored proteins in the plasma membrane form homodimer rafts via ectodomain protein interactions. Raft-lipid interactions stabilize higher order oligomers, which trigger intracellular signaling upon ligand binding.

See also: News and Views by Silvius

Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in tissue genesis   pp784 - 790
Gautam Bhave, Christopher F Cummings, Roberto M Vanacore, Chino Kumagai-Cresse, Isi A Ero-Tolliver, Mohamed Rafi, Jeong-Suk Kang, Vadim Pedchenko, Liselotte I Fessler, John H Fessler and Billy G Hudson
doi:10.1038/nchembio.1038



Peroxidasin uses hypohalous acid oxidants to catalyze the formation of sulfilimine bonds in basement membranes.

See also: News and Views by Weiss

A stand-alone adenylation domain forms amide bonds in streptothricin biosynthesis   pp791 - 797
Chitose Maruyama, Junya Toyoda, Yasuo Kato, Miho Izumikawa, Motoki Takagi, Kazuo Shin-ya, Hajime Katano, Takashi Utagawa and Yoshimitsu Hamano
doi:10.1038/nchembio.1040



A study of three synthetases involved in streptothricin biosynthesis demonstrates roles for two A domains in activating lysine, with one A domain transferring lysine to a carrier T domain and the second directly catalyzing amide bond formation to form a growing lysine oligopeptide.
Chemical compounds

A role for the root cap in root branching revealed by the non-auxin probe naxillin    pp798 - 805
Bert De Rybel, Dominique Audenaert, Wei Xuan, Paul Overvoorde, Lucia C Strader, Stefan Kepinski, Rebecca Hoye, Ronald Brisbois, Boris Parizot, Steffen Vanneste, Xing Liu, Alison Gilday, Ian A Graham, Long Nguyen, Leentje Jansen, Maria Fransiska Njo, Dirk Inzé, Bonnie Bartel and Tom Beeckman
doi:10.1038/nchembio.1044



The plant hormone auxin affects many aspects of root development, including lateral root branching. A high-throughput screen in Arabidopsis thaliana has led to the identification of naxillin, a non-auxin chemical probe that enhances lateral root branching and has revealed an important role of the root cap in regulating this process.
Chemical compounds

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