Dataset Information

Crystallization and preliminary X-ray crystallographic analysis of the complex between the N-D1 domain of VCP from Homo sapiens and the N domain of OTU1 from Saccharomyces cerevisiae.

ABSTRACT: VCP (valosin-containing protein; also known as p97) plays important roles in many biological processes including the ERAD (endoplasmic reticulum-associated degradation) pathway and its function is governed by binding partners. OTU1 (ovarian tumour domain-containing protein 1) is a recently discovered deubiquitinating enzyme that interacts directly with VCP in the ERAD pathway. In order to understand the interactions between the two proteins, the N-D1 domain of VCP and the UBXL domain of OTU1 were cloned, overexpressed, purified and crystallized. The crystals of the complex diffracted to 3.25?Å resolution and belonged to space group P21, with unit-cell parameters a = 165.45, b = 176.73, c = 165.59?Å, ? = 120.095°. There are two molecules of the complex in the asymmetric unit with a Matthews coefficient of 2.62?Å(3)?Da(-1) and a solvent content of 53%.

SUBMITTER: Kim SJ

PROVIDER: S-EPMC4118810 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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Publications

Crystallization and preliminary X-ray crystallographic analysis of the complex between the N-D1 domain of VCP from Homo sapiens and the N domain of OTU1 from Saccharomyces cerevisiae.

Kim Su Jin SJ Kim Eunice EunKyeong EE

Acta crystallographica. Section F, Structural biology communications 20140723 Pt 8

VCP (valosin-containing protein; also known as p97) plays important roles in many biological processes including the ERAD (endoplasmic reticulum-associated degradation) pathway and its function is governed by binding partners. OTU1 (ovarian tumour domain-containing protein 1) is a recently discovered deubiquitinating enzyme that interacts directly with VCP in the ERAD pathway. In order to understand the interactions between the two proteins, the N-D1 domain of VCP and the UBXL domain of OTU1 wer ...[more]

PMID: 25084388

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Project description:BackgroundMitochondria are thought to have evolved from eubacteria-like endosymbionts; however, the origin of the mitochondrion remains a subject of debate. In this study, we investigated the phenomenon of chimerism in mitochondria to shed light on the origin of these organelles by determining which species played a role in their formation. We used the mitochondria of four distinct organisms, Reclinomonas americana, Homo sapiens, Saccharomyces cerevisiae and multichromosome Pediculus humanus, and attempted to identify the origin of each mitochondrial gene.ResultsOur results suggest that the origin of mitochondrial genes is not limited to the Rickettsiales and that the creation of these genes did not occur in a single event, but through multiple successive events. Some of these events are very old and were followed by events that are more recent and occurred through the addition of elements originating from current species. The points in time that the elements were added and the parental species of each gene in the mitochondrial genome are different to the individual species. These data constitute strong evidence that mitochondria do not have a single common ancestor but likely have numerous ancestors, including proto-Rickettsiales, proto-Rhizobiales and proto-Alphaproteobacteria, as well as current alphaproteobacterial species. The analysis of the multichromosome P. humanus mitochondrion supports this mechanism.ConclusionsThe most plausible scenario of the origin of the mitochondrion is that ancestors of Rickettsiales and Rhizobiales merged in a proto-eukaryotic cell approximately one billion years ago. The fusion of the Rickettsiales and Rhizobiales cells was followed by gene loss, genomic rearrangements and the addition of alphaproteobacterial elements through ancient and more recent recombination events. Each gene of each of the four studied mitochondria has a different origin, while in some cases, multichromosomes may allow for enhanced gene exchange. Therefore, the tree of life is not sufficient to explain the chimeric structure of current genomes, and the theory of a single common ancestor and a top-down tree does not reflect our current state of knowledge. Mitochondrial evolution constitutes a rhizome, and it should be represented as such.

Dataset Information

Crystallization and preliminary X-ray crystallographic analysis of the complex between the N-D1 domain of VCP from Homo sapiens and the N domain of OTU1 from Saccharomyces cerevisiae.

Publications

Crystallization and preliminary X-ray crystallographic analysis of the complex between the N-D1 domain of VCP from Homo sapiens and the N domain of OTU1 from Saccharomyces cerevisiae.

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