Now showing items 1-17 of 17

    • 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 (Oxford University Press, 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 ...
      Journal article
    • 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 (BioMed Central, 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 ...
      Journal article
    • Depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and ARFRP1 localization 

      Starheim, Kristian K.; Kalvik, Thomas Vikestad; Bjørkøy, Geir; Arnesen, Thomas (Portland Press, 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 ...
      Journal article
    • 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 (Nature Publishing Group, 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 ...
      Journal article
    • First Things First: Vital Protein Marks by N-Terminal Acetyltransferases 

      Aksnes, Henriette; Drazic, Adrian; Marie, Michael Bruno Eric; Arnesen, Thomas (Elsevier, 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 ...
      Journal article
    • 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 (BioMed Central, 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 ...
      Journal article
    • 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 (Public Library of Science, 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 ...
      Peer reviewedJournal article
    • 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. (BioMed Central, 2011-09-19)
      Conference object
    • 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 (Portland Press Limited, 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 ...
      Journal article
    • N-terminal modifications of cellular proteins: the enzymes involved, their substrate specificities and biological effects 

      Varland, Sylvia; Osberg, Camilla; Arnesen, Thomas (Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, 2015-06-16)
      The vast majority of eukaryotic proteins are N-terminally modified by one or more processing enzymes. Enzymes acting on the very first amino acid of a polypeptide include different peptidases, transferases, and ligases. ...
      Journal article
    • NAA10 mutation causing a novel intellectual disability syndrome with Long QT due to N-terminal acetyltransferase impairment 

      Casey, Jillian P.; Støve, Svein Isungset; McGorrian, Catherine; Galvin, Joseph; Blenski, Marina; Dunne, Aimee; Ennis, Sean; Brett, Francesca; King, Mary D.; Arnesen, Thomas; Lynch, Sally Ann (Nature Publishing Group, 2015-11-02)
      We report two brothers from a non-consanguineous Irish family presenting with a novel syndrome characterised by intellectual disability, facial dysmorphism, scoliosis and long QT. Their mother has a milder phenotype including ...
      Journal article
    • NatF Contributes to an Evolutionary Shift in Protein N-Terminal Acetylation and Is Important for Normal Chromosome Segregation 

      Van Damme, Petra; Hole, Kristine; Pimenta-Marques, Ana; Helsens, Kenny; Vandekerckhove, Joël; Martinho, Rui G.; Gevaert, Kris; Arnesen, Thomas (Public Library of Science, 2011-07-07)
      N-terminal acetylation (N-Ac) is a highly abundant eukaryotic protein modification. Proteomics revealed a significant increase in the occurrence of N-Ac from lower to higher eukaryotes, but evidence explaining the underlying ...
      Peer reviewedJournal article
    • A novel human NatA N-alpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1) 

      Arnesen, Thomas; Gromyko, Darina; Kagabo, Diane; Betts, Matthew J.; Starheim, Kristian Kobbenes; Varhaug, Jan Erik; Anderson, Dave; Lillehaug, Johan (BioMed Central, 2009-05-29)
      Background: Protein acetylation is among the most common protein modifications. The two major types are post-translational Nε-lysine acetylation catalyzed by KATs (Lysine acetyltransferases, previously named HATs (histone ...
      Journal articlePeer reviewed
    • De novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and females 

      Popp, Bernt; Støve, Svein Isungset; Endele, Sabine; Myklebust, Line Merethe; Hoyer, Juliane; Sticht, Heinrich; Azzarello-Burri, Silvia; Rauch, Anita; Arnesen, Thomas; Reis, André (Nature Publishing Group, 2015)
      Recent studies revealed the power of whole-exome sequencing to identify mutations in sporadic cases with non-syndromic intellectual disability. We now identified de novo missense variants in NAA10 in two unrelated individuals, ...
      Journal article
    • The protein N-alpha-terminal acetyltransferase hNaa10p (hArd1) is phosphorylated in HEK293 cells 

      Målen, Hiwa; Lillehaug, Johan; Arnesen, Thomas (BioMed Central, 2009-03-02)
      Background: The hNaa10p (hArd1) protein is the catalytic subunit of the human NatA Nα- terminal acetyltransferase complex. The NatA complex is associated with ribosomes and cotranslationally acetylates human proteins ...
      Journal article
    • Specificity and Versatility of Substrate Binding Sites in Four Catalytic Domains of Human N-Terminal Acetyltransferases 

      Grauffel, Cédric; Abboud, Angèle; Liszczak, Glen; Marmorstein, Ronen; Arnesen, Thomas; Reuter, Nathalie (Public Library of Science, 2012-12-28)
      Nt-acetylation is among the most common protein modifications in eukaryotes. Although thought for a long time to protect proteins from degradation, the role of Nt-acetylation is still debated. It is catalyzed by enzymes ...
      Peer reviewedJournal article
    • Towards a Functional Understanding of Protein NTerminal Acetylation 

      Arnesen, Thomas (Public Library of Science, 2011-05-31)
      Protein N-terminal acetylation is a major modification of eukaryotic proteins. Its functional implications include regulation of protein–protein interactions and targeting to membranes, as demonstrated by studies of ...
      Peer reviewedJournal article