Substrate-assisted enzymatic formation of lysinoalanine in duramycin

September 3rd, 2018 by Linna An

Substrate-assisted enzymatic formation of lysinoalanine in duramycin

Substrate-assisted enzymatic formation of lysinoalanine in duramycin, Published online: 03 September 2018; doi:10.1038/s41589-018-0122-4

During the biosynthesis of the lanthipeptide duramycin, DurN catalyzes stereospecific lysinoalanine formation by preorganizing the reactive conformation of the substrate, such that one of the substrate’s own residues serves as the catalytic base.

Chemical proteomics reveals new targets of cysteine sulfinic acid reductase

September 3rd, 2018 by Salma Akter

Chemical proteomics reveals new targets of cysteine sulfinic acid reductase

Chemical proteomics reveals new targets of cysteine sulfinic acid reductase, Published online: 03 September 2018; doi:10.1038/s41589-018-0116-2

An electrophilic diazene probe (DiaAlk) enables capture and proteomic analysis of cysteine S-sulfinylation modifications, thus illuminating dynamic responses to oxidative stress and enabling the identification of new substrates of sulfiredoxin.
  • Posted in Nat Chem Biol, Publications
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Nuclear RNR-α antagonizes cell proliferation by directly inhibiting ZRANB3

August 27th, 2018 by Yuan Fu

Nuclear RNR-α antagonizes cell proliferation by directly inhibiting ZRANB3

Nuclear RNR-α antagonizes cell proliferation by directly inhibiting ZRANB3, Published online: 27 August 2018; doi:10.1038/s41589-018-0113-5

The large subunit of ribonucleotide reductase RNR-α downregulates DNA replication in the nucleus by directly disrupting PCNA and ZRANB3 interactions. RNR-α nuclear entry is regulated by an interplay between IRBIT and importin-α1.
  • Posted in Nat Chem Biol, Publications
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Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis

August 27th, 2018 by Takaaki Taniguchi

Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis

Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis, Published online: 27 August 2018; doi:10.1038/s41589-018-0119-z

A comparative genomic approach identified a novel acetate-dependent tRNA-modifying enzyme that catalyzes RNA acetylation with a mechanism similar to tRNA aminoacylation. This modification maintains decoding fidelity in protein synthesis.
  • Posted in Nat Chem Biol, Publications
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Continuous directed evolution of proteins with improved soluble expression

August 20th, 2018 by Tina Wang

Continuous directed evolution of proteins with improved soluble expression

Continuous directed evolution of proteins with improved soluble expression, Published online: 20 August 2018; doi:10.1038/s41589-018-0121-5

Through use of a split-intein pIII, soluble expression phage-assisted continuous evolution (SE-PACE) enables two simultaneous positive selections to rapidly evolve proteins with improved expression while maintaining their desired activities.
  • Posted in Nat Chem Biol, Publications
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<i>O</i>-GlcNAc modification of eIF4GI acts as a translational switch in heat shock response

August 20th, 2018 by Xingqian Zhang

O-GlcNAc modification of eIF4GI acts as a translational switch in heat shock response

<i>O</i>-GlcNAc modification of eIF4GI acts as a translational switch in heat shock response, Published online: 20 August 2018; doi:10.1038/s41589-018-0120-6

O-GlcNAcylation of translation initiation factor component eIF4GI blocks interactions to poly(A)-binding protein Pab1 to induce disassembly of stress granules, releasing Hsp70-induced mRNAs and leading to translation of protective proteins
  • Posted in Nat Chem Biol, Publications
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Catch and identify your prey

August 17th, 2018 by Karin Kuehnel

Catch and identify your prey

Catch and identify your prey, Published online: 17 August 2018; doi:10.1038/s41589-018-0125-1

Catch and identify your prey

A ribonucleotide trap

August 17th, 2018 by Yiyun Song

A ribonucleotide trap

A ribonucleotide trap, Published online: 17 August 2018; doi:10.1038/s41589-018-0127-z

A ribonucleotide trap

<i>ykkC</i> riboswitches employ an add-on helix to adjust specificity for polyanionic ligands

August 17th, 2018 by Alla Peselis

ykkC riboswitches employ an add-on helix to adjust specificity for polyanionic ligands

<i>ykkC</i> riboswitches employ an add-on helix to adjust specificity for polyanionic ligands, Published online: 17 August 2018; doi:10.1038/s41589-018-0114-4

Structural analysis of PRPP and ppGpp riboswitches reveals that they employ a helical element to create a tunnel for the ligand, whose specificity is determined by the conserved nucleotides forming the tunnel and long-distance contacts.
  • Posted in Nat Chem Biol, Publications
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TA gets a PG rating

August 17th, 2018 by Mirella Bucci

TA gets a PG rating

TA gets a PG rating, Published online: 17 August 2018; doi:10.1038/s41589-018-0126-0

TA gets a PG rating