N-terminal acetylation promotes synaptonemal complex assembly in C. elegans.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Gao, J; Barroso, C; Zhang, P; Kim, H-M; Li, S; Labrador, L; Lightfoot, J; Gerashchenko, MV; Labunskyy, VM; Dong, M-Q; Martinez-Perez, E; Colaiácovo, MP

Published Date

  • November 14, 2016

Published In

Volume / Issue

  • 30 / 21

Start / End Page

  • 2404 - 2416

PubMed ID

  • 27881602

Pubmed Central ID

  • PMC5131780

Electronic International Standard Serial Number (EISSN)

  • 1549-5477

International Standard Serial Number (ISSN)

  • 0890-9369

Digital Object Identifier (DOI)

  • 10.1101/gad.277350.116


  • eng