PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases

doi:10.1016/0092-8674(91)90234-P

Cell

Volume 64, Issue 3, 8 February 1991, Pages 499-510

https://doi.org/10.1016/0092-8674(91)90234-P Get rights and content

Abstract

PAS genes are required for peroxisome biogenesis in the yeast S. cerevisise. Here we describe the cloning, sequencing, and characterization of the PAS1 gene. Its gene product, Pas1p, has been identified as a rather hydrophilic 117 kd polypeptide. The predicted Pas1p sequence contains two putative ATP-binding sites and reveals a structural relationship to three other groups of proteins associated with different biological processes such as vesicle-mediated protein transport (NSF and Sec18p), control of cell cycle (Cdc48p, VCP, and p97-ATPase), and modulation of gene expression of the human Immunodeficiency virus (TBP-1). The proteins share a highly conserved domain of about 185 amino acids Including a consensus sequence for ATP binding. We suggest that these proteins are members of a novel family of putative ATPases and may be descendants of one common ancestor.

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P97 is a molecular chaperone evolutionally conserved in plants, yeasts and animals. This protein is a highly abundant ATPase of the AAA + family, defined as ‘ATPases Associated with diverse cellular Activities’ [1,2]. The mammalian homologue of plant and yeast CDC48 (Cell Division Cycle 48), called VCP (valosin-containing protein) in mammals, is one of the most abundant proteins in eukaryotic cells, accounting for 1% of cytosolic proteins [3,4].
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In particular, the by far most abundant Pex1pG843D variation impairs the binding between Pex1p and Pex6p [18–20]. Interestingly, Pex1p was the first peroxin identified in the early 90s [21] and shares a highly conserved ATP-binding domain with NSF (N-ethylmaleimide-sensitive factor) [22] and VCP (valosin-containing protein) [23]. This led to a classification of a new family of ATPases; the AAA-type ATPases [21,24,25], which also included the second peroxisomal AAA-peroxin Pex6p [26].
Mutations in the PEX1 gene, which encodes a protein required for peroxisome biogenesis, are the most common cause of the Zellweger spectrum diseases. The recognition that Pex1p shares a conserved ATP-binding domain with p97 and NSF led to the discovery of the extended family of AAA⁺-type ATPases. So far, four AAA⁺-type ATPases are related to peroxisome function. Pex6p functions together with Pex1p in peroxisome biogenesis, ATAD1/Msp1p plays a role in membrane protein targeting and a member of the Lon-family of proteases is associated with peroxisomal quality control. This review summarizes the current knowledge on the AAA⁺-proteins involved in peroxisome biogenesis and function. This article is part of a Special Issue entitled: Peroxisomes edited by Ralf Erdmann.

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^∗: Present address: Institute of Biochemistry and Biophysics, Polish Academy of Science, Rakowiecka, 02-532 Warsaw, Poland.

^†: Present address: Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler Strasse 4, 7400 Tübingen, Federal Republic of Germany.

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Cell

ArticlePAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases

Abstract

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Current Protocols in Molecular Biology

Specificity of DNA uptake during whole cell transformation of S. cerevisiae

Yeast

SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum

J. Cell Biol.

Relationships of human protein sequences to those of other organisms

Characterization of a component of the yeast secretion machinery: identification of the SEC18 gene product

Mol. Cell. Biol.

Article
PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases