Acetyltransferases articles within Nature Communications

Featured

• Article
  06 March 2024 | Open Access

  Microtubule damage shapes the acetylation gradient

  Microtubules are acetylated on the inside of their hollow lumen, a modification linked to their lifespan. Here, the authors show that damage holes act as entry points for a deacetylase to access the lumen, thereby locally counteracting acetylation.

  • Mireia Andreu-Carbó
  • , Cornelia Egoldt
  •  & Charlotte Aumeier

• Article
  17 February 2024 | Open Access

  Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells

  Here the authors report a strategy to directly capture substrates of lysine-modifying enzymes via post-translational modification (PTM)-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner.

  • Hao Hu
  • , Wei Hu
  •  & Xiao-Hua Chen

• Article
  27 October 2023 | Open Access

  N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity

  The most common protein modification in eukaryotes is N-terminal acetylation, but its functional impact has remained enigmatic. Here, the authors find that a key role for N-terminal acetylation is shielding proteins from ubiquitin ligase-mediated degradation, mediating motility and longevity.

  • Sylvia Varland
  • , Rui Duarte Silva
  •  & Thomas Arnesen

• Article
  25 September 2023 | Open Access

  Characterization and structure-based protein engineering of a regiospecific saponin acetyltransferase from Astragalus membranaceus

  Currently little is known about the acetylation on sugar moieties. Here the authors report a saponin acetyltransferase from Astragalus membranaceus, AmAT7-3, and utilise crystal structures and QM/MM computation to elucidate the catalytic mechanism: they generate mutants for specific site acetylation.

  • Linlin Wang
  • , Zhihui Jiang
  •  & Xue Qiao

• Article
  08 June 2023 | Open Access

  A crucial role for dynamic expression of components encoding the negative arm of the circadian clock

  A screen for clock mutants uncovered a conserved novel auxiliary NuA4 histone acetylase complex, containing orthologs of BRD-8 and BYE-1, needed for maintaining the timely Negative Element expression required for sustaining a normal circadian rhythm.

  • Bin Wang
  • , Xiaoying Zhou
  •  & Jay C. Dunlap

• Article
  26 November 2021 | Open Access

  Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction

  How is acetyl-CoA produced in the context of the endogenous, eukaryotic pyruvate dehydrogenase complex metabolon? Here the authors dissect the embedded transacetylase reaction through biochemical, cryo-EM, HADDOCKing and molecular dynamics methods.

  • Christian Tüting
  • , Fotis L. Kyrilis
  •  & Panagiotis L. Kastritis

• Article
  09 July 2021 | Open Access

  mTORC1 activity regulates post-translational modifications of glycine decarboxylase to modulate glycine metabolism and tumorigenesis

  An increase in glycine decarboxylase (GLDC) activity, a key enzyme for glycine catabolism, has been associated to tumourigenesis. Here, the authors show that mTORC1 activation induces GLDC deacetylation which impairs its ubiquitin-associated degradation leading to increased GLDC activity and tumourigenesis.

  • Rui Liu
  • , Lin-Wen Zeng
  •  & Shu Li

• Article
  17 October 2019 | Open Access

  Histone H3K23-specific acetylation by MORF is coupled to H3K14 acylation

  Acetylation of histone H3K23 has emerged as an essential posttranslational modification, yet this epigenetic mark remains poorly understood. Here, the authors identify the native MORF complex as a histone H3K23-specific acetyltransferase and show that interaction of the MORF subunit with acylated H3K14 promotes acetylation of H3K23 by this complex to activate transcription.

  • Brianna J. Klein
  • , Suk Min Jang
  •  & Tatiana G. Kutateladze

• Article
  06 June 2017 | Open Access

  Structural basis of HypK regulating N-terminal acetylation by the NatA complex

  N-terminal acetylation is a common eukaryotic protein modification that is primarily catalysed by the N-acetyl transferase complex A (NatA). Here, the authors present the crystal structure of NatA bound to Huntingtin yeast two-hybrid protein K (HypK) and show that HypK is a negative regulator of NatA.

  • Felix Alexander Weyer
  • , Andrea Gumiero
  •  & Irmgard Sinning

• Article
  17 July 2015 | Open Access

  Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis

  N-terminal acetylation is a common protein modification in eukaryotes. Here the authors show that in Arabidopsis, N-terminal acetylation is decreased by drought stress, that abundance of an N-terminal acetyltransferase is reduced by abscisic acid and that constitutive downregulation can confer drought resistance.

  • Eric Linster
  • , Iwona Stephan
  •  & Markus Wirtz