ACS DIVISION OF BIOLOGICAL CHEMISTRY

February 14th, 2018 by Kristoffer E Johansson

Protein evolution: Hacking an enzyme

Protein evolution: Hacking an enzyme, Published online: 14 February 2018; doi:10.1038/nchembio.2574

Early stages of protein evolution are inherently difficult to study. Genetic selection in Escherichia coli has now identified a life-sustaining de novo enzyme arising from a simple scaffold that is completely different from the native enzyme.

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.

February 9th, 2018 by Digvijay Singh and Taekjip Ha

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

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

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.

February 1st, 2018 by Parthiban Marimuthu and Kalaimathy Singaravelu

January 29th, 2018 by Hao Yin

Partial DNA-guided Cas9 enables genome editing with reduced off-target activity

Partial DNA-guided Cas9 enables genome editing with reduced off-target activity, Published online: 29 January 2018; doi:10.1038/nchembio.2559

Partial substitution of CRISPR RNAs with DNA nucleotides retains CRISPR–Cas9 genome editing activity while enhancing efficiency and specificity within cells, suggesting that DNA–RNA hybrids may be economical reagents for targeted genome editing.

January 29th, 2018 by ZeNan L Chang

Rewiring T-cell responses to soluble factors with chimeric antigen receptors

Rewiring T-cell responses to soluble factors with chimeric antigen receptors, Published online: 29 January 2018; doi:10.1038/nchembio.2565

Chimeric antigen receptor (CAR)-expressing T cells were engineered to recognize soluble protein ligands that, by inducing CAR dimerization, mechanically couple ligand binding and receptor signaling to produce immune effector molecules.

January 29th, 2018 by Marie Couturier

Lytic xylan oxidases from wood-decay fungi unlock biomass degradation

Lytic xylan oxidases from wood-decay fungi unlock biomass degradation, Published online: 29 January 2018; doi:10.1038/nchembio.2558

A new type of fungal lytic polysaccharide monooxygenase (LPMO) catalyzes the oxidative degradation of xylan components of cellulosic biomass and offers potential in wood biorefining.