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Nature Structural & Molecular Biology
Journal Prestige (SJR): 10.873
Citation Impact (citeScore): 10
Number of Followers: 217  
 
  Full-text available via subscription Subscription journal
ISSN (Print) 1545-9993 - ISSN (Online) 1545-9985
Published by NPG Homepage  [140 journals]
  • tRNA recycling on stalled ribosomes
    • tRNA recycling on stalled ribosomes

      tRNA recycling on stalled ribosomes, Published online: 22 April 2019; doi:10.1038/s41594-019-0222-1

      In the ribosome-associated quality control (RQC) pathway, stalled ribosomes are ubiquitinated and dissociated into subunits. The nascent protein chain associated with the 60S ribosomal subunit is ubiquitinated by the E3 ligase Listerin (Ltn1) and is released from tRNA by ANKZF1 (Vms1) for proteasomal degradation. Shao and colleagues now report that ANKZF1 (Vms1)-cleaved tRNAs are recycled via a two-step process that requires the removal of a terminal 2′,3′-cyclic phosphate and the addition of CCA by TRNT1.tRNA recycling on stalled ribosomes, Published online: 2019-04-22; doi:10.1038/s41594-019-0222-12019-04-22
      DOI: 10.1038/s41594-019-0222-1
       
  • Mechanism for recycling tRNAs on stalled ribosomes
    • Mechanism for recycling tRNAs on stalled ribosomes

      Mechanism for recycling tRNAs on stalled ribosomes, Published online: 22 April 2019; doi:10.1038/s41594-019-0211-4

      During ribosome-associated quality control (RQC), ANKZF1 severs polypeptidyl-tRNAs on RQC complexes by cleaving the terminal 3′CCA nucleotides, which leads to tRNA fragments that are ‘quality checked’ and recycled in the cytosol.Mechanism for recycling tRNAs on stalled ribosomes, Published online: 2019-04-22; doi:10.1038/s41594-019-0211-42019-04-22
      DOI: 10.1038/s41594-019-0211-4
       
  • Protein shapes at the core of chronic traumatic encephalopathy
    • Protein shapes at the core of chronic traumatic encephalopathy

      Protein shapes at the core of chronic traumatic encephalopathy, Published online: 22 April 2019; doi:10.1038/s41594-019-0221-2

      A recent cryo-EM study has generated breakthrough insights into the molecular and structural bases of tau tangles from individuals who died of CTE.Protein shapes at the core of chronic traumatic encephalopathy, Published online: 2019-04-22; doi:10.1038/s41594-019-0221-22019-04-22
      DOI: 10.1038/s41594-019-0221-2
       
  • Resolution of a complex crisis at DNA 3′ termini
    • Resolution of a complex crisis at DNA 3′ termini

      Resolution of a complex crisis at DNA 3′ termini, Published online: 15 April 2019; doi:10.1038/s41594-019-0215-0

      Ribonucleotides that are misincorporated into DNA during replication are removed by topoisomerase 1, which generates 3′-terminal adducts that are not amenable to DNA repair and thus compromise genome stability. A recent report by Li et al. reveals that Apn2/APE2 resolves such blocked 3′ termini, thereby suppressing topoisomerase 1–induced mutations at ribonucleotide monophosphate sites within the genome.Resolution of a complex crisis at DNA 3′ termini, Published online: 2019-04-15; doi:10.1038/s41594-019-0215-02019-04-15
      DOI: 10.1038/s41594-019-0215-0
       
  • A symmetric toggle switch explains the onset of random X inactivation in
           different mammals
    • A symmetric toggle switch explains the onset of random X inactivation in different mammals

      A symmetric toggle switch explains the onset of random X inactivation in different mammals, Published online: 08 April 2019; doi:10.1038/s41594-019-0214-1

      Mathematical modeling and experimental validation uncovers the minimal regulatory network that ensures stable mono-allelic expression of Xist.A symmetric toggle switch explains the onset of random X inactivation in different mammals, Published online: 2019-04-08; doi:10.1038/s41594-019-0214-12019-04-08
      DOI: 10.1038/s41594-019-0214-1
       
  • Broad-spectrum enzymatic inhibition of CRISPR-Cas12a
    • Broad-spectrum enzymatic inhibition of CRISPR-Cas12a

      Broad-spectrum enzymatic inhibition of CRISPR-Cas12a, Published online: 01 April 2019; doi:10.1038/s41594-019-0208-z

      Doudna and colleagues determine the mechanisms used by type V anti-CRISPR proteins. AcrVA1 is a multiple-turnover inhibitor that triggers cleavage of the Cas12a-bound guide RNA, while AcrVA4 and AcrVA5 inhibit recognition of dsDNA.Broad-spectrum enzymatic inhibition of CRISPR-Cas12a, Published online: 2019-04-01; doi:10.1038/s41594-019-0208-z2019-04-01
      DOI: 10.1038/s41594-019-0208-z
       
  • Enzymatic anti-CRISPRs improve the bacteriophage arsenal
    • Enzymatic anti-CRISPRs improve the bacteriophage arsenal

      Enzymatic anti-CRISPRs improve the bacteriophage arsenal, Published online: 01 April 2019; doi:10.1038/s41594-019-0210-5

      Bacteriophage-encoded anti-CRISPR (Acr) proteins were previously thought to inhibit CRISPR-mediated immunity by acting as physical barriers against the binding or cleavage of DNA. Two new studies report that recently discovered type V Acr proteins use enzymatic activities to shut down the Cas12a endonuclease, providing a multi-turnover ‘off switch’ for CRISPR-based immunity and technology.Enzymatic anti-CRISPRs improve the bacteriophage arsenal, Published online: 2019-04-01; doi:10.1038/s41594-019-0210-52019-04-01
      DOI: 10.1038/s41594-019-0210-5
       
  • An anti-CRISPR protein disables type V Cas12a by acetylation
    • An anti-CRISPR protein disables type V Cas12a by acetylation

      An anti-CRISPR protein disables type V Cas12a by acetylation, Published online: 01 April 2019; doi:10.1038/s41594-019-0206-1

      Zhiwei Huang and colleagues report structural and biochemical data showing that the anti-CRISPR protein AcrVA5 functions as an acetyltransferase, modifying MbCas12a at Lys635, a residue required for PAM recognition. Acetylation of Lys635 creates a steric clash that prevents binding of target DNA.An anti-CRISPR protein disables type V Cas12a by acetylation, Published online: 2019-04-01; doi:10.1038/s41594-019-0206-12019-04-01
      DOI: 10.1038/s41594-019-0206-1
       
 
 
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