The 2.8å Crystal Structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae : a five-layered αβαβα structure constructed from two core domains of identical topology

Mathieu, Magali; Zeelen, J.P.; Pauptit, Richard A.; Erdmann, Ralf; Kunau, Wolf‐H.; Wierenga, Rik K.

doi:10.1016/s0969-2126(94)00081-6

Cited by 89 publications

(98 citation statements)

References 43 publications

(39 reference statements)

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“…Recently, Mathieu et al (1994) published the crystal structure of peroxisomal OACT from S. cerevisiae refined at 2.8-A resolution. Apparently, the homodimeric unliganded yeast OACT comprises three domains: two compact core domains that have the same fold and a loop domain.…”

Section: Discussionmentioning

confidence: 99%

“…When hybridizations were performed under less-stringent conditions, however, more signals could be detected in all lanes (not shown). This would be expected in view of the presence of strongly conserved regions in all AACT and OACT sequences isolated so far (see Kanayama et al, 1994;Mathieu et al, 1994). However, at this stage we would not exclude the presence of related Figure 3.…”

Section: Genomic Dna Gel Blot Hybridization Analysismentioning

confidence: 91%

Section: Sequence Analysismentioning

confidence: 99%

“…The other, located at the C-terminal extremity (corresponding to Cys 390 in radish AACT; see Fig. 2), is the active site base involved in deprotonation in the condensation reaction (see Thompson et al, 1989;Williams et al, 1992;Mathieu et al, 1994, for discussion and further literature citations). The hydropathy profile of the deduced amino acid sequence of radish AACT, calculated according to Kyte and Doolittle (1982), exhibits the typical features of a soluble protein with internal hydrophobic core domains (not shown).…”

Section: Sequence Analysismentioning

confidence: 99%

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Cloning of a cDNA Encoding Cytosolic Acetoacetyl-Coenzyme A Thiolase from Radish by Functional Expression in Saccharomyces cerevisiae

Vollack

Bach

1996

Plant Physiology

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A cDNA coding for radish (Rapbanus sativus 1.) acetoacetylcoenzyme A thiolase (AACT) was cloned by complementation of the erglO mutation affecting AACT in yeast (Saccharomyces cerevisiae). l h e longest reading frame encodes a protein of 406 amino acids with a predicted relative molecular weight of 42,032, with significant similarities to eukaryotic and prokaryotic thiolases. lhere is no evidence for the presence of a leader peptide characteristic, e.g. of glyoxysomal thiolase. Yeast transformants expressing the radish AACT gene placed under the control of the CAL1 promoter exhibited a l O-fold higher enzyme activity than a wild-type yeast strain after induction by galactose. This enzyme activity is exclusively localized in the soluble fraction but not in membranes. These data indicate that we have cloned a gene encoding cytoplasmic (biosynthetic) AACT. Cenomic DNA gel blot analysis suggests the presence of a single AACT gene, which is expressed in all parts of the seedling. Expression in cotyledons appears to be lightstimulated. We present preliminary evidence that a smaller transcript represents an antisense species being read from the same gene.

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Section: Discussionmentioning

confidence: 99%

Section: Genomic Dna Gel Blot Hybridization Analysismentioning

confidence: 91%

Section: Sequence Analysismentioning

confidence: 99%

Section: Sequence Analysismentioning

confidence: 99%

See 2 more Smart Citations

Cloning of a cDNA Encoding Cytosolic Acetoacetyl-Coenzyme A Thiolase from Radish by Functional Expression in Saccharomyces cerevisiae

Vollack

Bach

1996

Plant Physiology

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“…Other PTS2-containing proteins dimerize or form higher multimers, suggesting that this may be a more general observation (Mathieu et al, 1994;Guex et al, 1995;Lee et al, 1997;Flynn et al, 1998;Chudzik et al, 2000). However, thiolase can be imported as a heterodimer when one subunit possesses a PTS2 and the other does not, which suggests that PTS2 dimerization is not required for import (Glover et al, 1994;Flynn et al, 1998).…”

Section: Pts2 Pathwaymentioning

confidence: 99%

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Lanyon‐Hogg

Warriner

Baker

2010

Biology of the Cell

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Peroxisomes are a family of organelles which have many unusual features. They can arise de novo from the endoplasmic reticulum by a still poorly characterized process, yet possess a unique machinery for the import of their matrix proteins. As peroxisomes lack DNA, their function, which is highly variable and dependent on developmental and/or environmental conditions, is determined by the post-translational import of specific metabolic enzymes in folded or oligomeric states. The two classes of matrix targeting signals for peroxisomal proteins [PTS1 (peroxisomal targeting signal 1) and PTS2] are recognized by cytosolic receptors [PEX5 (peroxin 5) and PEX7 respectively] which escort their cargo proteins to, or possibly across, the peroxisome membrane. Although the membrane translocation mechanism remains unclear, it appears to be driven by thermodynamically favourable binding interactions. Recycling of the receptors from the peroxisome membrane requires ATP hydrolysis for two linked processes: ubiquitination of PEX5 (and the PEX7 co-receptors in yeast) and the function of two peroxisome-associated AAA (ATPase associated with various cellular activities) ATPases, which play a role in recycling or turnover of the ubiquitinated receptors. This review summarizes and integrates recent findings on peroxisome matrix protein import from yeast, plant and mammalian model systems, and discusses some of the gaps in our understanding of this remarkable protein transport system.

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Structural trees for protein superfamilies

Ефимов

1997

Proteins

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Structural trees for large protein superfamilies, such as beta proteins with the aligned beta sheet packing, beta proteins with the orthogonal packing of alpha helices, two-layer and three-layer alpha/beta proteins, have been constructed. The structural motifs having unique overall folds and a unique handedness are taken as root structures of the trees. The larger protein structures of each superfamily are obtained by a stepwise addition of alpha helices and/or beta strands to the corresponding root motif, taking into account a restricted set of rules inferred from known principles of the protein structure. Among these rules, prohibition of crossing connections, attention to handedness and compactness, and a requirement for alpha helices to be packed in alpha-helical layers and beta strands in beta layers are the most important. Proteins and domains whose structures can be obtained by stepwise addition of alpha helices and/or beta strands to the same root motif can be grouped into one structural class or a superfamily. Proteins and domains found within branches of a structural tree can be grouped into subclasses or subfamilies. Levels of structural similarity between different proteins can easily be observed by visual inspection. Within one branch, protein structures having a higher position in the tree include the structures located lower. Proteins and domains of different branches have the structure located in the branching point as the common fold.

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The 2.8å Crystal Structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae : a five-layered αβαβα structure constructed from two core domains of identical topology

Cited by 89 publications

References 43 publications

Cloning of a cDNA Encoding Cytosolic Acetoacetyl-Coenzyme A Thiolase from Radish by Functional Expression in Saccharomyces cerevisiae

Cloning of a cDNA Encoding Cytosolic Acetoacetyl-Coenzyme A Thiolase from Radish by Functional Expression in Saccharomyces cerevisiae

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Structural trees for protein superfamilies

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