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Biochemical Characterisation of the Short Isoform of Histone N-Terminal Acetyltransferase NAA40.
Klavaris, Ariel; Kouma, Maria; Ozdemir, Cem; Nicolaidou, Vicky; Miller, Kyle M; Koufaris, Costas; Kirmizis, Antonis.
Afiliação
  • Klavaris A; Epigenetics and Gene Regulation Laboratory, Department of Biological Sciences, University of Cyprus, Nicosia 2109, Cyprus.
  • Kouma M; Epigenetics and Gene Regulation Laboratory, Department of Biological Sciences, University of Cyprus, Nicosia 2109, Cyprus.
  • Ozdemir C; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
  • Nicolaidou V; Department of Life Sciences, University of Nicosia, Nicosia 2417, Cyprus.
  • Miller KM; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
  • Koufaris C; Epigenetics and Gene Regulation Laboratory, Department of Biological Sciences, University of Cyprus, Nicosia 2109, Cyprus.
  • Kirmizis A; Cyprus Cancer Research Institute, Nicosia 2109, Cyprus.
Biomolecules ; 14(9)2024 Sep 02.
Article em En | MEDLINE | ID: mdl-39334865
ABSTRACT
N-alpha-acetyltransferase 40 (NAA40) is an evolutionarily conserved N-terminal acetyltransferase (NAT) linked to oncogenesis and chemoresistance. A recent study reported the generation of a second, shorter NAA40 isoform (NAA40S) through alternative translation, which we proceeded to further characterise. Notably, recombinant NAA40S had a greater in vitro enzymatic activity and affinity towards its histone H2A/H4 substrates compared to full-length NAA40 (NAA40L). Within cells, NAA40S was enzymatically active, based on its ability to suppress the H2A/H4S1Ph antagonistic mark in CRISPR-generated NAA40 knockout cells. Finally, we show that in addition to alternative translation, the NAA40S isoform could be derived from a primate and testis-specific transcript, which may align with the "out-of-testis" origin of recently evolved genes and isoforms. To summarise, our data reveal an even greater functional divergence between the two NAA40 isoforms than had been previously recognised.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Histonas Limite: Animals / Humans Idioma: En Revista: Biomolecules Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Chipre País de publicação: Suíça
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Histonas Limite: Animals / Humans Idioma: En Revista: Biomolecules Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Chipre País de publicação: Suíça