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Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters

Roerig, P, Mayerhofer, P, Holzinger, A and Gartner, J (2001) Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters FEBS Lett, 492. pp. 66-72.

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Abstract

The 70-kDa peroxisomal membrane protein (PMP70) and the adrenoleukodystrophy protein (ALDP) are half ATP binding cassette (ABC) transporters in the peroxisome membrane. Mutations in the ALD gene encoding ALDP result in the X-linked neurodegenerative disorder adrenoleukodystrophy. Plausible models exist to show a role for ATP hydrolysis in peroxisomal ABC transporter functions. Here, we describe the first measurements of the rate of ATP binding and hydrolysis by purified nucleotide binding fold (NBF) fusion proteins of PMP70 and ALDP. Both proteins act as an ATP specific binding subunit releasing ADP after ATP hydrolysis; they did not exhibit GTPase activity. Mutations in conserved residues of the nucleotidases (PMP70: G478R, S572I; ALDP: G512S, S606L) altered ATPase activity. Furthermore, our results indicate that these mutations do not influence homodimerization or heterodimerization of ALDP or PMP70. The study provides evidence that peroxisomal ABC transporters utilize ATP to become a functional transporter.

Item Type: Article
Authors :
NameEmailORCID
Roerig, PUNSPECIFIEDUNSPECIFIED
Mayerhofer, Pp.mayerhofer@surrey.ac.ukUNSPECIFIED
Holzinger, AUNSPECIFIEDUNSPECIFIED
Gartner, JUNSPECIFIEDUNSPECIFIED
Date : 2001
Uncontrolled Keywords : ATP-Binding Cassette Transporters/chemistry/genetics/*metabolism Adenosine Triphosphatases/metabolism Adenosine Triphosphate/*metabolism Amino Acid Motifs Amino Acid Sequence Animals Escherichia coli GTP Phosphohydrolases/metabolism Humans Membrane Proteins/chemistry/genetics/metabolism Molecular Sequence Data Peroxisomes/*metabolism Rabbits Recombinant Fusion Proteins/chemistry Sequence Homology, Amino Acid
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 10:42
Last Modified : 17 May 2017 14:51
URI: http://epubs.surrey.ac.uk/id/eprint/828858

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