Blar i Department of Biological Sciences på forfatter "Arnesen, Thomas"
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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 ... -
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 ... -
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 ... -
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 ... -
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 poster, 2011-09-19) -
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 ... -
N-terminal modifications of cellular proteins: the enzymes involved, their substrate specificities and biological effects
Varland, Sylvia; Osberg, Camilla; Arnesen, Thomas (Peer reviewed; Journal article, 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. ... -
NAA10 dysfunction with normal NatA-complex activity in a girl with non-syndromic ID and a de novo NAA10 p.(V111G) variant - a case report
Mc Tiernan, Nina; Støve, Svein Isungset; Aukrust, Ingvild; Mårli, Marita Torrissen; Myklebust, Line Merethe; Houge, Gunnar; Arnesen, Thomas (Peer reviewed; Journal article, 2018)Background: The NAA10-NAA15 (NatA) protein complex is an N-terminal acetyltransferase responsible for acetylating ~ 40% of eukaryotic proteins. In recent years, NAA10 variants have been found in patients with an X-linked ... -
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 (Peer reviewed; Journal article, 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 ... -
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 (Peer reviewed; Journal article, 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 ... -
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 (Peer reviewed; Journal article, 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 ... -
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 (Peer reviewed; Journal article, 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, ... -
The protein N-alpha-terminal acetyltransferase hNaa10p (hArd1) is phosphorylated in HEK293 cells
Målen, Hiwa; Lillehaug, Johan; Arnesen, Thomas (Peer reviewed; Journal article, 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 ... -
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 (Peer reviewed; Journal article, 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 ... -
Towards a Functional Understanding of Protein NTerminal Acetylation
Arnesen, Thomas (Peer reviewed; Journal article, 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 a ...