Browsing Bergen Open Research Archive by Author "Arnesen, Thomas"
Now showing items 21-40 of 41
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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 ... -
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
Varland, Sylvia; Silva, Rui Duarte; Kjosås, Ine; Faustino, Alexandra; Bogaert, Annelies; Billmann, Maximilian; Boukhatmi, Hadi; Kellen, Barbara; Costanzo, Michael; Drazic, Adrian; Osberg, Camilla; Chan, Katherine; Zhang, Xiang; Tong, Amy Hin Yan; Andreazza, Simonetta; Lee, Juliette J.; Nedyalkova, Lyudmila; Ušaj, Matej; Whitworth, Alexander J.; Andrews, Brenda J.; Moffat, Jason; Myers, Chad L.; Gevaert, Kris; Boone, Charles; Martinho, Rui Gonçalo; Arnesen, Thomas (Journal article; Peer reviewed, 2023)Most eukaryotic proteins are N-terminally acetylated, but the functional impact on a global scale has remained obscure. Using genome-wide CRISPR knockout screens in human cells, we reveal a strong genetic dependency between ... -
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 ... -
NAA10 p.(D10G) and NAA10 p.(L11R) variants hamper formation of the NatA N-terminal acetyltransferase complex
Mc Tiernan, Nina; Darbakk, Christine; Ree, Rasmus; Arnesen, Thomas (Journal article; Peer reviewed, 2020)The majority of the human proteome is subjected to N-terminal (Nt) acetylation catalysed by N-terminal acetyltransferases (NATs). The NatA complex is composed of two core subunits—the catalytic subunit NAA10 and the ribosomal ... -
NAA10 p.(N101K) disrupts N-terminal acetyltransferase complex NatA and is associated with developmental delay and hemihypertrophy
Mc Tiernan, Nina; Gill, Harinder; Prada, Carlos E.; Pachajoa, Harry; Lores, Juliana; Arnesen, Thomas (Journal article; Peer reviewed, 2020)Nearly half of all human proteins are acetylated at their N-termini by the NatA N-terminal acetyltransferase complex. NAA10 is evolutionarily conserved as the catalytic subunit of NatA in complex with NAA15, but may also ... -
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 ... -
A novel NAA10 p.(R83H) variant with impaired acetyltransferase activity identified in two boys with ID and microcephaly
Ree, Rasmus Moen; Geithus, Anni Sofie; Tørring, Pernille Mathiesen; Sørensen, Kristina Pilekær; Damkjær, Mads; Lynch, Sally Ann; Arnesen, Thomas (Peer reviewed; Journal article, 2019-06-07)Background N-terminal acetylation is a common protein modification in human cells and is catalysed by N-terminal acetyltransferases (NATs), mostly cotranslationally. The NAA10-NAA15 (NatA) protein complex is the major NAT, ... -
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, ... -
Optimized bisubstrate inhibitors for the actin N-terminal acetyltransferase NAA80
Myklebust, Line Merethe; Baumann, Markus; Støve, Svein Isungset; Foyn, Håvard; Arnesen, Thomas; Haug, Bengt Erik (Journal article; Peer reviewed, 2023)Acetylation of protein N-termini is one of the most common protein modifications in the eukaryotic cell and is catalyzed by the N-terminal acetyltransferase family of enzymes. The N-terminal acetyltransferase NAA80 is ... -
An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic n termini of transmembrane proteins and maintains golgi integrity
Aksnes, Henriette; Van Damme, Petra; Goris, Marianne; Starheim, Kristian K.; Marie, Michael Bruno Eric; Støve, Svein Isungset; Hoel, Camilla; Kalvik, Thomas Vikestad; Hole, Kristine; Glomnes, Nina; Furnes, Clemens; Ljostveit, Sonja; Ziegler, Mathias; Niere, Marc; Gevaert, Kris; Arnesen, Thomas (Peer reviewed; Journal article, 2015-02-26)N-terminal acetylation is a major and vital protein modification catalyzed by N-terminal acetyltransferases (NATs). NatF, or Nα-acetyltransferase 60 (Naa60), was recently identified as a NAT in multicellular eukaryotes. ... -
PFN2 and NAA80 cooperate to efficiently acetylate the N-terminus of actin
Reed, Rasmus; Kind, Laura; Kaziales, Anna; Varland, Sylvia; Dai, Minglu; Richter, Klaus; Drazic, Adrian; Arnesen, Thomas (Journal article; Peer reviewed, 2020)The actin cytoskeleton is of profound importance to cell shape, division, and intracellular force generation. Profilins bind to globular (G-)actin and regulate actin filament formation. Although profilins are well-established ... -
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 ... -
Structural and biophysical characterization of transcription factor HNF-1A as a tool to study MODY3 diabetes variants
Kind, Laura; Raasakka, Arne; Molnes, Janne; Aukrust, Ingvild; Bjørkhaug, Lise; Njølstad, Pål Rasmus; Kursula, Petri; Arnesen, Thomas (Journal article; Peer reviewed, 2022)Hepatocyte nuclear factor 1A (HNF-1A) is a transcription factor expressed in several embryonic and adult tissues, modulating the expression of numerous target genes. Pathogenic variants in the HNF1A gene are known to cause ... -
Structural properties of the HNF-1A transactivation domain
Kind, Laura; Driver, Mark; Raasakka, Arne; Onck, Patrick R.; Njølstad, Pål Rasmus; Arnesen, Thomas; Kursula, Petri Tapani (Journal article; Peer reviewed, 2023)Hepatocyte nuclear factor 1α (HNF-1A) is a transcription factor with important gene regulatory roles in pancreatic β-cells. HNF1A gene variants are associated with a monogenic form of diabetes (HNF1A-MODY) or an increased ... -
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 ...