Blar i Department of Biomedicine på forfatter "Arnesen, Thomas"
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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 ... -
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 ... -
Expanded in vivo substrate profile of the yeast N-terminal acetyltransferase NatC
Van Damme, Petra; Osberg, Camilla; Jonckheere, Veronique; Glomnes, Nina; Gevaert, Kris; Arnesen, Thomas; Aksnes, Henriette (Journal article; Peer reviewed, 2022)N-terminal acetylation is a conserved protein modification among eukaryotes. The yeast Saccharomyces cerevisiae is a valuable model system for studying this modification. The bulk of protein N-terminal acetylation in S. ... -
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 ... -
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, ... -
Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae
Guzman, Ulises H.; Aksnes, Henriette; Ree, Rasmus; Krogh, Nicolai; Jakobsson, Magnus; Jensen, Lars J.; Arnesen, Thomas; Olsen, Jesper V. (Journal article; Peer reviewed, 2023)Protein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes ... -
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 ... -
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 ... -
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, ... -
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 ... -
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 ...