Elongator protein 3 (Elp3) lysine acetyltransferase is a tail-anchored mitochondrial protein in toxoplasma gondii

Krista L. Stilger; William J. Sullivan

doi:10.1074/jbc.M113.491373

Elongator protein 3 (Elp3) lysine acetyltransferase is a tail-anchored mitochondrial protein in toxoplasma gondii

Krista L. Stilger, William J. Sullivan

Pharmacology & Toxicology

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

Background: Protein acetylation is prevalent in mitochondria, yet acetyltransferases mediating this activity are unknown. Results: Toxoplasma Elongator protein 3 (Elp3) possesses a unique C-terminal transmembrane domain necessary and sufficient to target it to the mitochondria. Conclusion: Elp3 is an essential tail-anchored mitochondrial acetyltransferase in Toxoplasma. Significance: Elp3 has conserved functions involving mitochondria that may predate its established role in transcription.

Original language	English (US)
Pages (from-to)	25318-25329
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	288
Issue number	35
DOIs	https://doi.org/10.1074/jbc.M113.491373
State	Published - Aug 30 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M113.491373

Fingerprint Dive into the research topics of 'Elongator protein 3 (Elp3) lysine acetyltransferase is a tail-anchored mitochondrial protein in toxoplasma gondii'. Together they form a unique fingerprint.

Cite this

@article{d0c3c0f5b2144e5386e286ae4cfbafac,

title = "Elongator protein 3 (Elp3) lysine acetyltransferase is a tail-anchored mitochondrial protein in toxoplasma gondii",

abstract = "Background: Protein acetylation is prevalent in mitochondria, yet acetyltransferases mediating this activity are unknown. Results: Toxoplasma Elongator protein 3 (Elp3) possesses a unique C-terminal transmembrane domain necessary and sufficient to target it to the mitochondria. Conclusion: Elp3 is an essential tail-anchored mitochondrial acetyltransferase in Toxoplasma. Significance: Elp3 has conserved functions involving mitochondria that may predate its established role in transcription.",

author = "Stilger, {Krista L.} and Sullivan, {William J.}",

year = "2013",

month = aug,

day = "30",

doi = "10.1074/jbc.M113.491373",

language = "English (US)",

volume = "288",

pages = "25318--25329",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "35",

}

TY - JOUR

T1 - Elongator protein 3 (Elp3) lysine acetyltransferase is a tail-anchored mitochondrial protein in toxoplasma gondii

AU - Stilger, Krista L.

AU - Sullivan, William J.

PY - 2013/8/30

Y1 - 2013/8/30

N2 - Background: Protein acetylation is prevalent in mitochondria, yet acetyltransferases mediating this activity are unknown. Results: Toxoplasma Elongator protein 3 (Elp3) possesses a unique C-terminal transmembrane domain necessary and sufficient to target it to the mitochondria. Conclusion: Elp3 is an essential tail-anchored mitochondrial acetyltransferase in Toxoplasma. Significance: Elp3 has conserved functions involving mitochondria that may predate its established role in transcription.

AB - Background: Protein acetylation is prevalent in mitochondria, yet acetyltransferases mediating this activity are unknown. Results: Toxoplasma Elongator protein 3 (Elp3) possesses a unique C-terminal transmembrane domain necessary and sufficient to target it to the mitochondria. Conclusion: Elp3 is an essential tail-anchored mitochondrial acetyltransferase in Toxoplasma. Significance: Elp3 has conserved functions involving mitochondria that may predate its established role in transcription.

UR - http://www.scopus.com/inward/record.url?scp=84883371503&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84883371503&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.491373

DO - 10.1074/jbc.M113.491373

M3 - Article

C2 - 23878194

AN - SCOPUS:84883371503

VL - 288

SP - 25318

EP - 25329

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 35

ER -