Vitamin B<sub>12</sub> import is all about timing

June 18th, 2018 by Lutz Schmitt

Vitamin B12 import is all about timing

Vitamin B<sub>12</sub> import is all about timing, Published online: 18 June 2018; doi:10.1038/s41589-018-0087-3

Single-molecule techniques combined with molecular dynamics simulations allowed visualization of a surprisingly high level of conformational homogeneity in the transport cycle of an ABC import system, BtuCD-F, and revealed an unexpected tight coupling of distinct conformational states responsible for vitamin B12 binding, transport and release.

The Jumonji-C oxygenase JMJD7 catalyzes (3<i>S</i>)-lysyl hydroxylation of TRAFAC GTPases

June 18th, 2018 by Suzana Markolovic

The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases

The Jumonji-C oxygenase JMJD7 catalyzes (3<i>S</i>)-lysyl hydroxylation of TRAFAC GTPases, Published online: 18 June 2018; doi:10.1038/s41589-018-0071-y

Structural, biochemical and cellular studies reveal JMJD7 to be a Jumonji-C oxygenase that catalyzes (3S)-lysyl hydroxylation of the translation factor family of GTPases, DRG1 and DRG2.
  • Posted in Nat Chem Biol, Publications
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The anti-staphylococcal lipolanthines are ribosomally synthesized lipopeptides

June 18th, 2018 by Vincent Wiebach

The anti-staphylococcal lipolanthines are ribosomally synthesized lipopeptides

The anti-staphylococcal lipolanthines are ribosomally synthesized lipopeptides, Published online: 18 June 2018; doi:10.1038/s41589-018-0068-6

The antibacterial microvionin contains two new lanthipeptide modifications, a triamino-dicarboxylic acid (avionin) and an N-terminal guanidino fatty acid, that lead to the establishment of the lipolanthine natural product class.
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Scavenging of superoxide by a membrane-bound superoxide oxidase

June 18th, 2018 by Camilla A. K. Lundgren

Scavenging of superoxide by a membrane-bound superoxide oxidase

Scavenging of superoxide by a membrane-bound superoxide oxidase, Published online: 18 June 2018; doi:10.1038/s41589-018-0072-x

The membrane-bound enzyme CybB can directly oxidize superoxide to molecular oxygen and transfer the sequestered electrons to ubiquinone in vitro, providing a mechanism for superoxide scavenging distinct from that of superoxide dismutase.

Single-molecule probing of the conformational homogeneity of the ABC transporter BtuCD

June 18th, 2018 by Min Yang

Single-molecule probing of the conformational homogeneity of the ABC transporter BtuCD

Single-molecule probing of the conformational homogeneity of the ABC transporter BtuCD, Published online: 18 June 2018; doi:10.1038/s41589-018-0088-2

A single-molecule approach combined with molecular dynamics simulations to examine the conformational dynamics of the Escherichia coli ABC transporter BtuCD defines a coordinated sequence of events leading to unidirectional transport.
  • Posted in Nat Chem Biol, Publications
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[ASAP] Charge Dispersion and Its Effects on the Reactivity of Thiamin-Derived Breslow Intermediates

June 14th, 2018 by Michael Bielecki, Graeme W. Howe, Ronald Kluger

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.8b00463

The RNA-binding complex ESCRT-II in Xenopus laevis eggs recognizes purine-rich sequences through its subunit Vps25 [Cell Biology]

June 14th, 2018 by Amy B Emerman, Michael Blower

RNA-binding proteins (RBPs) are critical regulators of gene expression. Recent studies have uncovered hundreds of mRNA-binding proteins that do not contain annotated RNA-binding domains and have well-established roles in other cellular processes. Investigation of these nonconventional RBPs is critical for revealing novel RNA-binding domains and may disclose connections between RNA regulation and other aspects of cell biology. Endosomal sorting complex required for transport II (ESCRT-II) is a nonconventional RNA-binding complex that has a canonical role in multivesicular body formation. ESCRT-II previously has been identified as an RNA-binding complex in Drosophila oocytes, but whether its RNA-binding properties extend beyond Drosophila is unknown. In this study, we found that the RNA-binding properties of ESCRT-II are conserved in Xenopus eggs, where ESCRT-II interacted with hundreds of mRNAs. Using a UV-crosslinking approach, we demonstrated that ESCRT-II binds directly to RNA through its subunit Vps25. UV-crosslinking and immunoprecipitation (CLIP)-Seq revealed that Vps25 specifically recognizes a polypurine (i.e. GA-rich) motif in RNA. Using purified components, we could reconstitute the selective Vps25-mediated binding of the polypurine motif in vitro. Our results provide insight into the mechanism by which ESCRT-II selectively binds to mRNAs and also suggest an unexpected link between endosome biology and RNA regulation.

Plasticity in binding confers selectivity in ligand-induced protein degradation

June 11th, 2018 by Radosław P. Nowak

Plasticity in binding confers selectivity in ligand-induced protein degradation

Plasticity in binding confers selectivity in ligand-induced protein degradation, Published online: 11 June 2018; doi:10.1038/s41589-018-0055-y

Selectivity of ligand-induced protein degradation and dimerization is conferred by plastic interprotein contacts. Computational protein–protein docking reveals the underlying interprotein contacts to inform the design of a BRD4 selective degrader.
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Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern

June 11th, 2018 by Benoit Castrec

Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern

Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern, Published online: 11 June 2018; doi:10.1038/s41589-018-0077-5

Aided by the solving of the structures of human NMT1 with substrate-mimicking peptides, mapping of human and Arabidopsis myristoylomes defines a myristoylation recognition motif and over 1,000 myristoylated protein targets.
  • Posted in Nat Chem Biol, Publications
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Linkers for protein degradation

June 11th, 2018 by Philip P. Chamberlain

Linkers for protein degradation

Linkers for protein degradation, Published online: 11 June 2018; doi:10.1038/s41589-018-0057-9

The ability to subvert E3 ubiquitin ligases with small-molecule drugs offers tremendous promise for drug discovery. A new study demonstrates how structural and computational techniques can engineer and exploit unnatural protein–protein interfaces to design selective protein degraders.