PloS one, 2013-08, Vol.8 (8), p.e71856-e71856
2013
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- Autor(en) / Beteiligte
- Titel
- A primate specific extra domain in the molecular chaperone Hsp90
- Ist Teil von
- PloS one, 2013-08, Vol.8 (8), p.e71856-e71856
- Ort / Verlag
- United States: Public Library of Science
- Erscheinungsjahr
- 2013
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Hsp90 (heat shock protein 90) is an essential molecular chaperone that mediates folding and quality control of client proteins. Many of them such as protein kinases, steroid receptors and transcription factors are involved in cellular signaling processes. Hsp90 undergoes an ATP hydrolysis dependent conformational cycle to assist folding of the client protein. The canonical Hsp90 shows a typical composition of three distinct domains and interacts with individual cochaperone partners such as Hop, Cdc37 and Aha1 (activator of Hsp90 ATPase) that regulate the reaction cycle of the molecular chaperone. A bioinformatic survey identified an additional domain of 122 amino acids in front of the canonical Hsp90 sequence. This extra domain (E domain) is specific to the Catarrhini or drooping nose monkeys, a subdivision of the higher primates that includes man, the great apes and the old world monkeys but is absent from all other species. Our biochemical analysis reveals that Hsp103 associates with cochaperone proteins such as Hop, Cdc37 and Aha1 similar to Hsp90. However, the extra domain reduces the ATP hydrolysis rate to about half when compared to Hsp90 thereby acting as a negative regulator of the molecular chaperonés intrinsic ATPase activity.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1932-6203eISSN: 1932-6203DOI: 10.1371/journal.pone.0071856Titel-ID: cdi_plos_journals_1430257053
- Format
- –
- Schlagworte
- Adenosine triphosphatase, Adenosine Triphosphatases - chemistry, Adenosine Triphosphatases - genetics, Adenosine Triphosphatases - metabolism, Adenosine Triphosphate - chemistry, Adenosine Triphosphate - metabolism, Amino Acid Sequence, Amino acids, Animals, Apes, ATP, ATPases, Biochemical analysis, Biology, Catarrhini - genetics, Catarrhini - metabolism, Cell cycle, Cell Cycle Proteins - genetics, Cell Cycle Proteins - metabolism, Chaperonins - genetics, Chaperonins - metabolism, Computational Biology, Cystic fibrosis, DNA binding proteins, Escherichia coli - genetics, Folding, Heat shock proteins, HEK293 Cells, Homeodomain Proteins - genetics, Homeodomain Proteins - metabolism, HSP90 Heat-Shock Proteins - chemistry, HSP90 Heat-Shock Proteins - classification, HSP90 Heat-Shock Proteins - genetics, HSP90 Heat-Shock Proteins - metabolism, Hsp90 protein, Humans, Hydrolysis, Kinases, Molecular Chaperones - genetics, Molecular Chaperones - metabolism, Molecular Sequence Data, Monkeys, Nose, Phylogeny, Physiology, Primates, Protein Binding, Protein folding, Protein Interaction Domains and Motifs, Protein kinase, Protein kinases, Proteins, Quality control, Receptors, Recombinant Proteins - chemistry, Recombinant Proteins - genetics, Recombinant Proteins - metabolism, Sequence Alignment, Signaling, Steroid hormone receptors, Transcription factors, Tumor Suppressor Proteins - genetics, Tumor Suppressor Proteins - metabolism