Altering form for function

February 14th, 2018 by Nature Chemical Biology - Issue - nature.com science feeds

Altering form for function

Altering form for function, Published online: 14 February 2018; doi:10.1038/nchembio.2582

Elucidating the mechanisms by which biomolecules are chemically modified and how these alterations regulate biological pathways represents a leading frontier in chemical biology.

Viruses: Capsids under pressure

February 14th, 2018 by Mirella Bucci

Viruses: Capsids under pressure

Viruses: Capsids under pressure, Published online: 14 February 2018; doi:10.1038/nchembio.2578

Viruses: Capsids under pressure

How many human proteoforms are there?

February 14th, 2018 by Ruedi Aebersold

How many human proteoforms are there?

How many human proteoforms are there?, Published online: 14 February 2018; doi:10.1038/nchembio.2576

How many human proteoforms are there?

Insights into the biogenesis, function, and regulation of ADP-ribosylation

February 14th, 2018 by Michael S Cohen

Insights into the biogenesis, function, and regulation of ADP-ribosylation

Insights into the biogenesis, function, and regulation of ADP-ribosylation, Published online: 14 February 2018; doi:10.1038/nchembio.2568

Insights into the biogenesis, function, and regulation of ADP-ribosylation
  • Posted in Nat Chem Biol, Publications
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RNA structure: A LASER-focused view into cells

February 14th, 2018 by Philip C Bevilacqua

RNA structure: A LASER-focused view into cells

RNA structure: A LASER-focused view into cells, Published online: 14 February 2018; doi:10.1038/nchembio.2570

RNA structure is irrevocably linked to function. A new method, termed 'LASER', utilizes a light-activated chemical probe to query RNA tertiary structure and illuminate RNA–protein interactions in the living cell.

The ABCs of PTMs

February 14th, 2018 by Karl W Barber

The ABCs of PTMs

The ABCs of PTMs, Published online: 14 February 2018; doi:10.1038/nchembio.2572

Post-translational modifications (PTMs) are ubiquitous in all forms of life and often modulate critical protein functions. Recent chemical and biological advances have finally enabled scientists to precisely modify proteins at physiologically relevant positions, ushering in a new era of protein studies.

Understanding the Molecular Mechanisms of the CRISPR Toolbox Using Single Molecule Approaches

February 9th, 2018 by Digvijay Singh and Taekjip Ha

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ACS Chemical Biology
DOI: 10.1021/acschembio.7b00905

Development of Activity-Based Chemical Probes for Human Sirtuins

February 8th, 2018 by Elysian Graham, Stacia Rymarchyk, Marci Wood and Yana Cen

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ACS Chemical Biology
DOI: 10.1021/acschembio.7b00754

Toward a Microparticle-Based System for Pooled Assays of Small Molecules in Cellular Contexts

February 8th, 2018 by Carrie E. Yozwiak, Tal Hirschhorn and Brent R. Stockwell

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ACS Chemical Biology
DOI: 10.1021/acschembio.8b00043

Ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I [Protein Synthesis and Degradation]

February 1st, 2018 by Lei Lei, Joanna Bandola-Simon, Paul A. Roche

March-I is a membrane-bound E3 ubiquitin ligase belonging to the membrane-associated RING-CH (March) family. March-I ubiquitinates and down-regulates expression of major histocompatibility complex (MHC) class II and cluster of differentiation 86 (CD86) in antigen presenting cells. March-I expression is regulated both transcriptionally and post-translationally and it has been reported that the March-I is ubiquitinated and that this ubiquitination contributes to March-I turnover. However, the molecular mechanism regulating March-I ubiquitination and the importance of March-I's E3 ligase activity for March-I ubiquitination are not fully understood. Here we confirmed that although March-I is ubiquitinated, it is not ubiquitinated on a lysine residue as a lysine-less March-I variant was ubiquitinated similarly to wild-type March-I. We found that March-I E3 ligase activity is not required for its ubiquitination and does not regulate March-I protein expression, suggesting that March-I does not undergo autoubiquitination. Knocking down ubiquitin-conjugating enzyme E2 D1 (Ube2D1) impaired March-I ubiquitination, increased March-I expression, and enhanced March-I-dependent downregulation of MHC class II proteins. Taken together, our results suggest that March-I undergoes lysine-independent ubiquitination by an as yet unidentified E3 ubiquitin ligase that together with Ube2D1 regulates March-I expression.
  • Posted in Journal of Biological Chemistry, Publications
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