Reference - Detail
| RRC ID | 33607 |
|---|---|
| Author | Fleckenstein T, Kastenmüller A, Stein ML, Peters C, Daake M, Krause M, Weinfurtner D, Haslbeck M, Weinkauf S, Groll M, Buchner J. |
| Title | The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational Changes. |
| Journal | Mol Cell |
| Abstract |
Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that prevent the aggregation of unfolding proteins during proteotoxic stress. In Caenorhabditis elegans, Sip1 is the only sHsp exclusively expressed in oocytes and embryos. Here, we demonstrate that Sip1 is essential for heat shock survival of reproducing adults and embryos. X-ray crystallography and electron microscopy revealed that Sip1 exists in a range of well-defined globular assemblies consisting of two half-spheres, each made of dimeric "spokes." Strikingly, the oligomeric distribution of Sip1 as well as its chaperone activity depend on pH, with a trend toward smaller species and higher activity at acidic conditions such as present in nematode eggs. The analysis of the interactome shows that Sip1 has a specific substrate spectrum including proteins that are essential for embryo development. |
| Volume | 58(6) |
| Pages | 1067-78 |
| Published | 2015-6-18 |
| DOI | 10.1016/j.molcel.2015.04.019 |
| PII | S1097-2765(15)00301-9 |
| PMID | 26009280 |
| MeSH | Amino Acid Sequence Animals Blotting, Western Caenorhabditis elegans / genetics Caenorhabditis elegans / metabolism Caenorhabditis elegans Proteins / chemistry* Caenorhabditis elegans Proteins / classification Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism Cryoelectron Microscopy Crystallography, X-Ray Heat-Shock Proteins, Small / chemistry* Heat-Shock Proteins, Small / genetics Heat-Shock Proteins, Small / metabolism Hydrogen-Ion Concentration Models, Molecular Molecular Chaperones / chemistry* Molecular Chaperones / genetics Molecular Chaperones / metabolism Molecular Sequence Data Mutation Phylogeny Protein Binding Protein Conformation* Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Sequence Homology, Amino Acid Temperature |
| IF | 15.584 |
| Times Cited | 29 |
| WOS Category | BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 15 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| C.elegans | tm3624 (sip-1 F43D9.4) |