title: N-terminal acetylation promotes synaptonemal complex assembly in C. elegans.
abstract: N-terminal acetylation of the first two amino acids on proteins is a prevalent cotranslational modification. Despite its abundance, the biological processes associated with this modification are not well understood. Here, we mapped the pattern of protein N-terminal acetylation in Caenorhabditis elegans, uncovering a conserved set of rules for this protein modification and identifying substrates for the N-terminal acetyltransferase B (NatB) complex. We observed an enrichment for global protein N-terminal acetylation and also specifically for NatB substrates in the nucleus, supporting the importance of this modification for regulating biological functions within this cellular compartment. Peptide profiling analysis provides evidence of cross-talk between N-terminal acetylation and internal modifications in a NAT substrate-specific manner. In vivo studies indicate that N-terminal acetylation is critical for meiosis, as it regulates the assembly of the synaptonemal complex (SC), a proteinaceous structure ubiquitously present during meiosis from yeast to humans. Specifically, N-terminal acetylation of NatB substrate SYP-1, an SC structural component, is critical for SC assembly. These findings provide novel insights into the biological functions of N-terminal acetylation and its essential role during meiosis.
authors.affiliation: Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: Jinmin
authors.initials: J
authors.lastname: Gao
authors.affiliation: Medical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
authors.forename: Consuelo
authors.initials: C
authors.lastname: Barroso
authors.affiliation: College of Life Science, Beijing Normal University, Beijing 100875, China; National Institute of Biological Sciences, Beijing 102206, China.
authors.forename: Pan
authors.initials: P
authors.lastname: Zhang
authors.affiliation: Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: Hyun-Min
authors.initials: HM
authors.lastname: Kim
authors.affiliation: College of Life Science, Beijing Normal University, Beijing 100875, China; National Institute of Biological Sciences, Beijing 102206, China.
authors.forename: Shangtong
authors.initials: S
authors.lastname: Li
authors.affiliation: Medical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
authors.forename: Leticia
authors.initials: L
authors.lastname: Labrador
authors.affiliation: Medical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
authors.forename: James
authors.initials: J
authors.lastname: Lightfoot
authors.affiliation: Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: Maxim V
authors.initials: MV
authors.lastname: Gerashchenko
authors.affiliation: Department of Dermatology, Boston University School of Medicine, Boston, Massachusetts 02218, USA.
authors.forename: Vyacheslav M
authors.initials: VM
authors.lastname: Labunskyy
authors.affiliation: College of Life Science, Beijing Normal University, Beijing 100875, China; National Institute of Biological Sciences, Beijing 102206, China.
authors.forename: Meng-Qiu
authors.initials: MQ
authors.lastname: Dong
authors.affiliation: Medical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
authors.forename: Enrique
authors.initials: E
authors.lastname: Martinez-Perez
authors.affiliation: Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: Monica P
authors.initials: MP
authors.lastname: Colaiácovo
mesh_terms: D000107:Acetylation; D000818:Animals; D017173:Caenorhabditis elegans / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D008540:Meiosis / Q000235:genetics; D009154:Mutation; D063210:N-Terminal Acetyltransferase B / Q000235:genetics / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism; D020543:Proteome; D013573:Synaptonemal Complex / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D029742:Caenorhabditis elegans Proteins; D009687:Nuclear Proteins; D020543:Proteome; C569962:SYP-1 protein, C elegans; D063210:N-Terminal Acetyltransferase B
keywords: C. elegans; N-terminal acetylation; NatB complex; meiosis; synaptonemal complex