N-terminal acetylation by NatC is not a general determinant for substrate subcellular localization in Saccharomyces cerevisiae

PLoS One. 2013 Apr 15;8(4):e61012. doi: 10.1371/journal.pone.0061012. Print 2013.

Abstract

N-terminal acetylation has been suggested to play a role in the subcellular targeting of proteins, in particular those acetylated by the N-terminal acetyltransferase complex NatC. Based on previous positional proteomics data revealing N-terminal acetylation status and the predicted NAT substrate classes, we selected 13 suitable NatC substrates for subcellular localization studies in Saccharomyces cerevisiae. Fluorescence microscopy analysis of GFP-tagged candidates in the presence or absence of the NatC catalytic subunit Naa30 (Mak3) revealed unaltered localization patterns for all 13 candidates, thus arguing against a general role for the N-terminal acetyl group as a localization determinant. Furthermore, all organelle-localized substrates indicated undisrupted structures, thus suggesting that absence of NatC acetylation does not have a vast effect on organelle morphology in yeast.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Amino Acid Sequence
  • Genomics
  • Green Fluorescent Proteins / metabolism
  • Intracellular Space / metabolism*
  • N-Terminal Acetyltransferase C / metabolism*
  • Protein Transport
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / metabolism

Substances

  • Green Fluorescent Proteins
  • N-Terminal Acetyltransferase C

Grant support

This work was supported by The Bergen Research Foundation, the Research Council of Norway (Grant 197136 to T.A) and the Norwegian Cancer Society. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.