Blar i Bergen Open Research Archive på forfatter "Mc Tiernan, Nina"
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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 ... -
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 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 ...