COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae

Christopher G. Carlson, Antonio Barrientos, Alexander Tzagoloff, D. Moira Glerum

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

We have characterized Cox16p, a new cytochrome oxidase (COX) assembly factor. This protein is encoded by COX16, corresponding to the previously uncharacter. ized open reading frame YJL003w of the yeast genome. COX16 was identified in studies of COX-deficient mutants previously assigned to complementation group G22 of a collection of yeast pet mutants. To determine its location, Cox16p was tagged with a Myc epitope at the C terminus. The fusion protein, when expressed from a low-copy plasmid, complements the mutant and is detected solely in mitochondria. Cox16p-myc is an integral component of the mitochondrial inner membrane, with its C terminus exposed to the intermembrane space. Cox16 homologues are found in both the human and murine genomes, although human COX16 does not complement the yeast mutant. Cox16p does not appear to be involved in maturation of subunit 2, copper recruit. ment, or heme A biosynthesis. Cox16p is thus a new protein in the growing family of eukaryotic COX assembly factors for which there are as yet no specific func. tions known. Like other recently described nuclear gene products involved in expression of cytochrome oxidase, COX16 is a candidate for screening in inherited human COX deficiencies.

Original languageEnglish
Pages (from-to)3770-3775
Number of pages6
JournalJournal of Biological Chemistry
Volume278
Issue number6
DOIs
StatePublished - Feb 7 2003
Externally publishedYes

Fingerprint

Electron Transport Complex IV
Yeast
Saccharomyces cerevisiae
Yeasts
Genes
Proteins
Cytochrome-c Oxidase Deficiency
Pets
Mitochondrial Membranes
Human Genome
Heme
Mitochondria
Open Reading Frames
Biosynthesis
Copper
Epitopes
Plasmids
Genome
Screening
Fusion reactions

ASJC Scopus subject areas

  • Biochemistry

Cite this

COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae. / Carlson, Christopher G.; Barrientos, Antonio; Tzagoloff, Alexander; Glerum, D. Moira.

In: Journal of Biological Chemistry, Vol. 278, No. 6, 07.02.2003, p. 3770-3775.

Research output: Contribution to journalArticle

Carlson, Christopher G. ; Barrientos, Antonio ; Tzagoloff, Alexander ; Glerum, D. Moira. / COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 6. pp. 3770-3775.
@article{4e444f99684a45eaa895b62e3db8771a,
title = "COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae",
abstract = "We have characterized Cox16p, a new cytochrome oxidase (COX) assembly factor. This protein is encoded by COX16, corresponding to the previously uncharacter. ized open reading frame YJL003w of the yeast genome. COX16 was identified in studies of COX-deficient mutants previously assigned to complementation group G22 of a collection of yeast pet mutants. To determine its location, Cox16p was tagged with a Myc epitope at the C terminus. The fusion protein, when expressed from a low-copy plasmid, complements the mutant and is detected solely in mitochondria. Cox16p-myc is an integral component of the mitochondrial inner membrane, with its C terminus exposed to the intermembrane space. Cox16 homologues are found in both the human and murine genomes, although human COX16 does not complement the yeast mutant. Cox16p does not appear to be involved in maturation of subunit 2, copper recruit. ment, or heme A biosynthesis. Cox16p is thus a new protein in the growing family of eukaryotic COX assembly factors for which there are as yet no specific func. tions known. Like other recently described nuclear gene products involved in expression of cytochrome oxidase, COX16 is a candidate for screening in inherited human COX deficiencies.",
author = "Carlson, {Christopher G.} and Antonio Barrientos and Alexander Tzagoloff and Glerum, {D. Moira}",
year = "2003",
month = "2",
day = "7",
doi = "10.1074/jbc.M209893200",
language = "English",
volume = "278",
pages = "3770--3775",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "6",

}

TY - JOUR

T1 - COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae

AU - Carlson, Christopher G.

AU - Barrientos, Antonio

AU - Tzagoloff, Alexander

AU - Glerum, D. Moira

PY - 2003/2/7

Y1 - 2003/2/7

N2 - We have characterized Cox16p, a new cytochrome oxidase (COX) assembly factor. This protein is encoded by COX16, corresponding to the previously uncharacter. ized open reading frame YJL003w of the yeast genome. COX16 was identified in studies of COX-deficient mutants previously assigned to complementation group G22 of a collection of yeast pet mutants. To determine its location, Cox16p was tagged with a Myc epitope at the C terminus. The fusion protein, when expressed from a low-copy plasmid, complements the mutant and is detected solely in mitochondria. Cox16p-myc is an integral component of the mitochondrial inner membrane, with its C terminus exposed to the intermembrane space. Cox16 homologues are found in both the human and murine genomes, although human COX16 does not complement the yeast mutant. Cox16p does not appear to be involved in maturation of subunit 2, copper recruit. ment, or heme A biosynthesis. Cox16p is thus a new protein in the growing family of eukaryotic COX assembly factors for which there are as yet no specific func. tions known. Like other recently described nuclear gene products involved in expression of cytochrome oxidase, COX16 is a candidate for screening in inherited human COX deficiencies.

AB - We have characterized Cox16p, a new cytochrome oxidase (COX) assembly factor. This protein is encoded by COX16, corresponding to the previously uncharacter. ized open reading frame YJL003w of the yeast genome. COX16 was identified in studies of COX-deficient mutants previously assigned to complementation group G22 of a collection of yeast pet mutants. To determine its location, Cox16p was tagged with a Myc epitope at the C terminus. The fusion protein, when expressed from a low-copy plasmid, complements the mutant and is detected solely in mitochondria. Cox16p-myc is an integral component of the mitochondrial inner membrane, with its C terminus exposed to the intermembrane space. Cox16 homologues are found in both the human and murine genomes, although human COX16 does not complement the yeast mutant. Cox16p does not appear to be involved in maturation of subunit 2, copper recruit. ment, or heme A biosynthesis. Cox16p is thus a new protein in the growing family of eukaryotic COX assembly factors for which there are as yet no specific func. tions known. Like other recently described nuclear gene products involved in expression of cytochrome oxidase, COX16 is a candidate for screening in inherited human COX deficiencies.

UR - http://www.scopus.com/inward/record.url?scp=0037423199&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037423199&partnerID=8YFLogxK

U2 - 10.1074/jbc.M209893200

DO - 10.1074/jbc.M209893200

M3 - Article

C2 - 12446688

AN - SCOPUS:0037423199

VL - 278

SP - 3770

EP - 3775

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 6

ER -