[ASAP] Programmed Allelic Mutagenesis of a DNA Polymerase with Single Amino Acid Resolution

June 29th, 2020 by

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ACS Synthetic Biology
DOI: 10.1021/acssynbio.0c00236

[ASAP] Physicochemical Tools for Visualizing and Quantifying Cell-Generated Forces

June 25th, 2020 by Ashley K. Nguyen and Kristopher A. Kilian*

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ACS Chemical Biology
DOI: 10.1021/acschembio.0c00304

Ubiquitination of interleukin-1{alpha} is associated with increased pro-inflammatory polarization of murine macrophages deficient in the E3 ligase ITCH [Cell Biology]

June 25th, 2020 by Xi Lin, Hengwei Zhang, Brendan F. Boyce, Lianping Xing

Macrophages play critical roles in homeostasis and inflammation. Macrophage polarization to either a pro-inflammatory or anti-inflammatory status is controlled by activating inflammatory signaling pathways. Ubiquitination is a post-translational modification that regulates these inflammatory signaling pathways. However, the influence of protein ubiquitination on macrophage polarization has not been well studied. We hypothesized that the ubiquitination status of key proteins in inflammatory pathways contributes to macrophage polarization, which is regulated by itchy E3 ubiquitin ligase (ITCH), a negative regulator of inflammation. Using ubiquitin proteomics, we found that ubiquitination profiles are different among polarized murine macrophage subsets. Interestingly, interleukin-1α (IL-1α), an important proinflammatory mediator, was specifically ubiquitinated in lipopolysaccharide-induced proinflammatory macrophages, which was enhanced in ITCH-deficient macrophages. The ITCH-deficient macrophages had increased levels of the mature form of IL-1α and exhibited proinflammatory polarization, and reduced deubiquitination of IL-1α protein. Finally, IL-1α neutralization attenuated pro-inflammatory polarization of the ITCH-deficient macrophages. In conclusion, ubiquitination of IL-1α is associated with increased pro-inflammatory polarization of macrophages deficient in the E3 ligase ITCH.
  • Posted in Journal of Biological Chemistry, Publications
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Publisher Correction: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family

June 25th, 2020 by Camila R. Santos

Nature Chemical Biology, Published online: 25 June 2020; doi:10.1038/s41589-020-0590-1

Publisher Correction: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family
  • Posted in Nat Chem Biol, Publications
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[ASAP] Artificial Protein-Responsive Riboswitches Upregulate Non-AUG Translation Initiation in Yeast

June 22nd, 2020 by Fumihiro Horie, Kei Endo*, and Koichi Ito*

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ACS Synthetic Biology
DOI: 10.1021/acssynbio.0c00206

[ASAP] Harnessing Natural Modularity of Metabolism with Goal Attainment Optimization to Design a Modular Chassis Cell for Production of Diverse Chemicals

June 22nd, 2020 by Sergio Garcia†‡ and Cong T. Trinh*†‡

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ACS Synthetic Biology
DOI: 10.1021/acssynbio.9b00518
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Groovy RNA polymerase

June 22nd, 2020 by Mirella Bucci

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0582-1

Groovy RNA polymerase

Dissecting the Pol II transcription cycle and derailing cancer with CDK inhibitors

June 22nd, 2020 by Pabitra K. Parua

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0563-4

This Review provides insights into transcriptional regulation, and vulnerabilities of cancer cells to disruption of cyclin-dependent kinase (CDK)-mediated regulation of Pol II transcription, revealed with small-molecule CDK inhibitors.
  • Posted in Nat Chem Biol, Publications
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Structural insight into the formation of lipoprotein-β-barrel complexes

June 22nd, 2020 by Raquel Rodríguez-Alonso

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0575-0

A structural and biochemical study of bacterial β-barrel assembly machinery component BamA with transport substrate RcsF shows an inward-open conformation with RcsF trapped inside the β-barrel lumen and suggests a push–pull substrate export mechanism.
  • Posted in Nat Chem Biol, Publications
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Spectroscopic coherent Raman imaging of <i>Caenorhabditis elegans</i> reveals lipid particle diversity

June 22nd, 2020 by Wei-Wen Chen

Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0565-2

A Raman-based imaging approach that can distinguish closely related chemical species used to characterize the distribution of lipids throughout the body of intact Caenorhabditis elegans worms shows that the epidermis is an important fat-storage reservoir.
  • Posted in Nat Chem Biol, Publications
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