• Biochemical analysis of novel NAA10 variants suggests distinct pathogenic mechanisms involving impaired protein N‑terminal acetylation 

      McTiernan, Nina; Tranebjærg, Lisbeth; Bjørheim, Anna Steensen; Hogue, Jacob S.; Wilson, William G.; Schmidt, Berkley; Boerrigter, Melissa M.; Nybo, Maja L.; Smeland, Marie; Tümer, Zeynep; Arnesen, Thomas (Journal article; Peer reviewed, 2022)
      NAA10 is the catalytic subunit of the N-terminal acetyltransferase complex, NatA, which is responsible for N-terminal acetylation of nearly half the human proteome. Since 2011, at least 21 different NAA10 missense variants ...
    • Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects 

      Myklebust, Line Merethe; Van Damme, Petra; Støve, Svein Isungset; Dörfel, Max J; Abboud, Angèle; Kalvik, Thomas Vikestad; Grauffel, Cédric; Jonckheere, Veronique; Wu, Yiyang; Swensen, Jeffrey; Kaasa, Hanna; Liszczak, Glen; Marmorstein, Ronen; Reuter, Nathalie; Lyon, Gholson J; Gevaert, Kris; Arnesen, Thomas (Peer reviewed; Journal article, 2014-12-03)
      The X-linked lethal Ogden syndrome was the first reported human genetic disorder associated with a mutation in an N-terminal acetyltransferase (NAT) gene. The affected males harbor an Ser37Pro (S37P) mutation in the gene ...
    • Characterization of Evolutionarily Conserved Trypanosoma cruzi NatC and NatA-N-Terminal Acetyltransferase Complexes 

      Ochaya, Stephen; Franzén, Oscar; Buhwa, Doreen Asiimwe; Foyn, Håvard; Butler, Claire E.; Støve, Svein Isungset; Tyler, Kevin M.; Arnesen, Thomas; Matovu, Enock; Åslund, Lena; Andersson, Bjørn (Peer reviewed; Journal article, 2019-03-06)
      Protein N-terminal acetylation is a co- and posttranslational modification, conserved among eukaryotes. It determines the functional fate of many proteins including their stability, complex formation, and subcellular ...
    • Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase 

      Arnesen, Thomas; Betts, Matthew J.; Pendino, Frédéric; Liberles, David A.; Anderson, Dave; Caro, Jaime; Kong, Xianguo; Varhaug, Jan Erik; Lillehaug, Johan (Peer reviewed; Journal article, 2006-04-25)
      Background: Protein acetylation is increasingly recognized as an important mechanism regulating a variety of cellular functions. Several human protein acetyltransferases have been characterized, most of them catalyzing ...
    • Classification and phylogeny for the annotation of novel eukaryotic GNAT acetyltransferases 

      Krtenic, Bojan; Drazic, Adrian; Arnesen, Thomas; Reuter, Nathalie (Journal article; Peer reviewed, 2020)
      The enzymes of the GCN5-related N-acetyltransferase (GNAT) superfamily count more than 870 000 members through all kingdoms of life and share the same structural fold. GNAT enzymes transfer an acyl moiety from acyl coenzyme ...
    • Co-translational, post-translational, and non-catalytic roles of N-terminal acetyltransferases 

      Aksnes, Henriette; Ree, Rasmus Moen; Arnesen, Thomas (Peer reviewed; Journal article, 2019)
      Recent studies of N-terminal acetylation have identified new N-terminal acetyltransferases (NATs) and expanded the known functions of these enzymes beyond their roles as ribosome-associated co-translational modifiers. For ...
    • Depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and ARFRP1 localization 

      Starheim, Kristian K.; Kalvik, Thomas Vikestad; Bjørkøy, Geir; Arnesen, Thomas (Peer reviewed; Journal article, 2017-04-28)
      The organization of the Golgi apparatus (GA) is tightly regulated. Golgi stack scattering is observed in cellular processes such as apoptosis and mitosis, and has also been associated with disruption of cellular lipid ...
    • Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis 

      Linster, Eric; Stephan, Iwona; Bienvenut, Willy V.; Maple-Grødem, Jodi; Myklebust, Line Merethe; Huber, Monika; Reichelt, Michael; Sticht, Carsten; Møller, Simon Geir; Meinnel, Thierry; Arnesen, Thomas; Giglione, Carmela; Hell, Rüdiger; Wirtz, Markus (Peer reviewed; Journal article, 2015-07-17)
      N-terminal acetylation (NTA) catalysed by N-terminal acetyltransferases (Nats) is among the most common protein modifications in eukaryotes, but its significance is still enigmatic. Here we characterize the plant NatA ...
    • Dynamics-function relationship in the catalytic domains of N-terminal acetyltransferases 

      Abboud, Angèle; Bedoucha, Pierre; Byska, Jan; Arnesen, Thomas; Reuter, Nathalie (Journal article; Peer reviewed, 2020)
      N-terminal acetyltransferases (NATs) belong to the superfamily of acetyltransferases. They are enzymes catalysing the transfer of an acetyl group from acetyl coenzyme A to the N-terminus of polypeptide chains. N-terminal ...
    • The Final Maturation State of β-actin Involves N-terminal Acetylation by NAA80, not N-terminal Arginylation by ATE1 

      Drazic, Adrian; Timmerman, Evy; Kajan, Ulrike; Marie, Michaël Bruno Eric; Varland, Sylvia; Impens, Francis; Gevaert, Kris; Arnesen, Thomas (Journal article; Peer reviewed, 2022)
      Actin is a hallmark protein of the cytoskeleton in eukaryotic cells, affecting a range of cellular functions. Actin dynamics is regulated through a myriad of actin-binding proteins and post-translational modifications. The ...
    • First Things First: Vital Protein Marks by N-Terminal Acetyltransferases 

      Aksnes, Henriette; Drazic, Adrian; Marie, Michael Bruno Eric; Arnesen, Thomas (Peer reviewed; Journal article, 2016-09)
      N-terminal (Nt) acetylation is known to be a highly abundant co-translational protein modification, but the recent discovery of Golgi- and chloroplast-resident N-terminal acetyltransferases (NATs) revealed that it can also ...
    • Functional evaluation of 16 SCHAD missense variants: Only amino acid substitutions causing congenital hyperinsulinism of infancy lead to loss-of-function phenotypes in vitro 

      Velasco Pinto, Kelly; St-Louis, Johanna; Hovland, Henrikke N.; Thompson, Nels; Ottesen, Åsta; Choi, Man Hung; Pedersen, Line; Njølstad, Pål Rasmus; Arnesen, Thomas; Fjeld, Karianne; Aukrust, Ingvild; Myklebust, Line Merethe; Molven, Anders (Journal article; Peer reviewed, 2021)
      Short‐chain 3‐hydroxyacyl‐CoA dehydrogenase (SCHAD), encoded by the HADH gene, is a ubiquitously expressed mitochondrial enzyme involved in fatty acid oxidation. This protein also plays a role in insulin secretion as ...
    • HIV-1 Rev oligomerization is not obligatory in the presence of an extra basic domain 

      Furnes, Clemens; Arnesen, Thomas; Askjaer, Peter; Kjems, Jørgen; Szilvay, Anne Marie (Peer reviewed; Journal article, 2005-06-10)
      Background: The HIV-1 Rev regulatory protein binds as an oligomeric complex to viral RNA mediating nuclear export of incompletely spliced and non-spliced viral mRNAs encoding the viral structural proteins. However, the ...
    • The Human N-Alpha-Acetyltransferase 40 (hNaa40p/ hNatD) Is Conserved from Yeast and N-Terminally Acetylates Histones H2A and H4 

      Hole, Kristine; Van Damme, Petra; Dalva, Monica; Aksnes, Henriette; Glomnes, Nina; Varhaug, Jan Erik; Lillehaug, Johan; Gevaert, Kris; Arnesen, Thomas (Peer reviewed; Journal article, 2011-09-15)
      Protein Na-terminal acetylation (Nt-acetylation) is considered one of the most common protein modification in eukaryotes, and 80-90% of all soluble human proteins are modified in this way, with functional implications ...
    • Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells 

      Ree, Rasmus Moen; Krogstad, Karoline; Jakobsson, Magnus E.; Arnesen, Thomas; McTiernan, Nina (Journal article; Peer reviewed, 2021)
      NAA10 is a major N-terminal acetyltransferase (NAT) that catalyzes the cotranslational N-terminal (Nt-) acetylation of 40% of the human proteome. Several reports of lysine acetyltransferase (KAT) activity by NAA10 exist, ...
    • Massively parallel sequencing identifies a previously unrecognized X-linked disorder resulting in lethality in male infants owing to amino-terminal acetyltransferase deficiency 

      Rope, Alan F.; Wang, Kai; Evjenth, Rune; Xing, Jinchuan; Johnston, Jennifer J.; Swensen, Jeffrey J.; Johnson, W. E.; Moore, Barry; Huff, Chad D.; Bird, Lynne M.; Carey, John C.; Opitz, John M.; Stevens, Cathy A.; Schank, Christa; Fain, Heidi D.; Robison, Reid; Dalley, Brian; Chin, Steven; South, Sarah T.; Pysher, Theodore J.; Jorde, Lynn B.; Hakonarson, Hakon; Lillehaug, Johan; Biesecker, Leslie G.; Yandell, Mark; Arnesen, Thomas; Lyon, Gholson J. (Conference object; Peer reviewed, 2011-09-19)
    • Mechanism of actin N-terminal acetylation 

      Rebowski, Grzegorz; Boczkowska, Malgorzata; Drazic, Adrian; Ree, Rasmus Moen; Goris, Marianne; Arnesen, Thomas; Dominguez, Roberto (Journal article; Peer reviewed, 2020)
      About 80% of human proteins are amino-terminally acetylated (Nt-acetylated) by one of seven Nt-acetyltransferases (NATs). Actin, the most abundant protein in the cytoplasm, has its own dedicated NAT, NAA80, which acts ...
    • Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK 

      Deng, Sunbin; Mc Tiernan, Nina; Wei, Xuepeng; Arnesen, Thomas; Marmorstein, Ronen (Journal article; Peer reviewed, 2020-02)
      The human N-terminal acetyltransferase E (NatE) contains NAA10 and NAA50 catalytic, and NAA15 auxiliary subunits and associates with HYPK, a protein with intrinsic NAA10 inhibitory activity. NatE co-translationally acetylates ...
    • N-terminal acetylation of actin by NAA80 is essential for structural integrity of the Golgi apparatus 

      Beigl, Tobias; Hellesvik, Monica; Saraste, Jaakko; Arnesen, Thomas; Aksnes, Henriette (Journal article; Peer reviewed, 2020)
      N-alpha-acetyltransferase 80 (NAA80) was recently demonstrated to acetylate the N-terminus of actin, with NAA80 knockout cells showing actin cytoskeleton-related phenotypes, such as increased formation of membrane protrusions ...
    • The N-terminal acetyltransferase Naa10 is essential for zebrafish development 

      Ree, Rasmus Moen; Myklebust, Line Merethe; Thiel, Puja; Foyn, Håvard; Fladmark, Kari Espolin; Arnesen, Thomas (Peer reviewed; Journal article, 2015-08-06)
      N-terminal acetylation, catalysed by N-terminal acetyltransferases (NATs), is among the most common protein modifications in eukaryotes and involves the transfer of an acetyl group from acetyl-CoA to the α-amino group of ...