Affinity-purification and identification of GrpE homologues from mammalian mitochondria

Dean J. Naylor; Michael T. Ryan; Rosemary Condron; Nicholas J. Hoogenraad; Peter B. Høj

doi:10.1016/0167-4838(95)00007-H

Affinity-purification and identification of GrpE homologues from mammalian mitochondria

Dean J. Naylor, Michael T. Ryan, Rosemary Condron, Nicholas J. Hoogenraad, Peter B. Høj

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

16 Citations (Scopus)

Abstract

We used affinity chromatography on DnaK columns to identify a mitochondrial GrpE homologue from bovine, porcine and rat liver mitochondria. The 24 kDa GrpE homologue bound specifically to the DnaK column and was not eluted with 1 M KCl but readily with 5 mM ATP. Sequence analysis of the bovine homologue (85 residues) revealed 42% positional identity to mitochondrial GrpEp from S. cerevisiae and about 30% identity to the bacterial counterparts. Thus, GrpE homologues from higher and lower eukaryotes are highly conserved.

Original language	English
Pages (from-to)	75-79
Number of pages	5
Journal	Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume	1248
Issue number	1
DOIs	https://doi.org/10.1016/0167-4838(95)00007-H
Publication status	Published - 5 Apr 1995
Externally published	Yes

Keywords

Chaperone
Protein sequencing

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10.1016/0167-4838(95)00007-H

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abstract = "We used affinity chromatography on DnaK columns to identify a mitochondrial GrpE homologue from bovine, porcine and rat liver mitochondria. The 24 kDa GrpE homologue bound specifically to the DnaK column and was not eluted with 1 M KCl but readily with 5 mM ATP. Sequence analysis of the bovine homologue (85 residues) revealed 42% positional identity to mitochondrial GrpEp from S. cerevisiae and about 30% identity to the bacterial counterparts. Thus, GrpE homologues from higher and lower eukaryotes are highly conserved.",

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AU - Naylor, Dean J.

AU - Ryan, Michael T.

AU - Condron, Rosemary

AU - Hoogenraad, Nicholas J.

AU - Høj, Peter B.

PY - 1995/4/5

Y1 - 1995/4/5

N2 - We used affinity chromatography on DnaK columns to identify a mitochondrial GrpE homologue from bovine, porcine and rat liver mitochondria. The 24 kDa GrpE homologue bound specifically to the DnaK column and was not eluted with 1 M KCl but readily with 5 mM ATP. Sequence analysis of the bovine homologue (85 residues) revealed 42% positional identity to mitochondrial GrpEp from S. cerevisiae and about 30% identity to the bacterial counterparts. Thus, GrpE homologues from higher and lower eukaryotes are highly conserved.

AB - We used affinity chromatography on DnaK columns to identify a mitochondrial GrpE homologue from bovine, porcine and rat liver mitochondria. The 24 kDa GrpE homologue bound specifically to the DnaK column and was not eluted with 1 M KCl but readily with 5 mM ATP. Sequence analysis of the bovine homologue (85 residues) revealed 42% positional identity to mitochondrial GrpEp from S. cerevisiae and about 30% identity to the bacterial counterparts. Thus, GrpE homologues from higher and lower eukaryotes are highly conserved.

KW - Chaperone

KW - Protein sequencing

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JO - Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

JF - Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

IS - 1

ER -

Affinity-purification and identification of GrpE homologues from mammalian mitochondria

Abstract

Keywords

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