論文 - 詳細
| RRC ID | 47224 |
|---|---|
| 著者 | Osberg C, Aksnes H, Ninzima S, Marie M, Arnesen T. |
| タイトル | Microscopy-based Saccharomyces cerevisiae complementation model reveals functional conservation and redundancy of N-terminal acetyltransferases. |
| ジャーナル | Sci Rep |
| Abstract |
N-terminal acetylation is a highly abundant protein modification catalyzed by N-terminal acetyltransferases (NATs) NatA-NatG. The Saccharomyces cerevisiae protein Arl3 depends on interaction with Sys1 for its localization to the Golgi and this targeting strictly requires NatC-mediated N-terminal acetylation of Arl3. We utilized the Arl3 acetylation-dependent localization phenotype as a model system for assessing the functional conservation and in vivo redundancy of several human NATs. The catalytic subunit of human NatC, hNaa30 (Mak3), restored Arl3 localization in the absence of yNaa30, but only in the presence of either yeast or human Naa35 subunit (Mak10). In contrast, hNaa35 was not able to replace its yeast orthologue without the co-expression of hNaa30, suggesting co-evolution of the two NatC subunits. The most recently discovered and organellar human NAT, NatF/Naa60, restored the Golgi localization of Arl3 in the absence of yNaa30. Interestingly, this was also true for hNaa60 lacking its membrane-binding domain whereas hNaa50 did not complement NatC function. This in vivo redundancy reflects NatC and NatF´s overlapping in vitro substrate specificities. The yeast model presented here provides a robust and rapid readout of NatC and NatF activity in vivo, and revealed evolutionary conservation of the NatC complex and redundancy between NatC and NatF. |
| 巻・号 | 6 |
| ページ | 31627 |
| 公開日 | 2016-8-24 |
| DOI | 10.1038/srep31627 |
| PII | srep31627 |
| PMID | 27555049 |
| PMC | PMC4995432 |
| MeSH | ADP-Ribosylation Factors / metabolism Acetylation Genetic Complementation Test Golgi Apparatus / metabolism Humans Microscopy, Fluorescence N-Terminal Acetyltransferases / physiology* Protein Processing, Post-Translational* Protein Transport Saccharomyces cerevisiae / genetics Saccharomyces cerevisiae / metabolism Saccharomyces cerevisiae / ultrastructure Saccharomyces cerevisiae Proteins / metabolism |
| IF | 3.998 |
| 引用数 | 0 |
| WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
|
| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 遺伝子材料 | 316-SEC7-mRFP (RDB08663) |