Self-association of a small heat shock protein.
Identifieur interne : 002E81 ( Main/Curation ); précédent : 002E80; suivant : 002E82Self-association of a small heat shock protein.
Auteurs : Barbara Lelj-Garolla [Canada] ; A Grant MaukSource :
- Journal of molecular biology [ 0022-2836 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Protéines du choc thermique.
- métabolisme : Protéines du choc thermique.
- Délétion de séquence, Humains, Mutagenèse dirigée, Ultracentrifugation.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Heat-Shock Proteins.
- chemical , metabolism : Heat-Shock Proteins.
- Humans, Mutagenesis, Site-Directed, Sequence Deletion, Ultracentrifugation.
Abstract
Human Hsp27 oligomerizes in vivo in a phosphorylation-dependent manner that regulates the functional activity of the protein. We have studied the self-association of wild-type Hsp27 by both sedimentation velocity and sedimentation equilibrium analysis and established that the protein forms an equilibrium mixture of monomers/dimers, tetramers, 12-mers and 16-mers (20 mM Tris-HCl (pH 8.4), 100 mM NaCl, 20 degrees C). Corresponding analysis of the S15D/S78D/S82D triple variant, which is believed to mimic the behavior of phosphorylated Hsp27, establishes that this form of the protein forms primarily monomers and dimers but also forms a small fraction of very large oligomers. Variants in which critical N-terminal sequences have been deleted exhibit oligomerization behavior that is intermediate between that of the triple variant and the wild-type protein. On the other hand a C-terminal sequence deletion variant forms larger oligomers than does the wild-type protein, but also exhibits a greater fraction of smaller oligomers. Notably, the presence of an N-terminal His6-tag induces formation of much larger oligomers than observed for any other form of the protein. The results of this work establish that the wild-type protein forms smaller oligomers than previously believed, define the roles played by various structural domains in Hsp27 oligomerization, and provide improved molecular probes with better-defined properties for the design of future experiments.
DOI: 10.1016/j.jmb.2004.10.056
PubMed: 15581903
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pubmed:15581903Le document en format XML
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<term>Ultracentrifugation</term>
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<term>Protéines du choc thermique (métabolisme)</term>
<term>Ultracentrifugation</term>
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<front><div type="abstract" xml:lang="en">Human Hsp27 oligomerizes in vivo in a phosphorylation-dependent manner that regulates the functional activity of the protein. We have studied the self-association of wild-type Hsp27 by both sedimentation velocity and sedimentation equilibrium analysis and established that the protein forms an equilibrium mixture of monomers/dimers, tetramers, 12-mers and 16-mers (20 mM Tris-HCl (pH 8.4), 100 mM NaCl, 20 degrees C). Corresponding analysis of the S15D/S78D/S82D triple variant, which is believed to mimic the behavior of phosphorylated Hsp27, establishes that this form of the protein forms primarily monomers and dimers but also forms a small fraction of very large oligomers. Variants in which critical N-terminal sequences have been deleted exhibit oligomerization behavior that is intermediate between that of the triple variant and the wild-type protein. On the other hand a C-terminal sequence deletion variant forms larger oligomers than does the wild-type protein, but also exhibits a greater fraction of smaller oligomers. Notably, the presence of an N-terminal His6-tag induces formation of much larger oligomers than observed for any other form of the protein. The results of this work establish that the wild-type protein forms smaller oligomers than previously believed, define the roles played by various structural domains in Hsp27 oligomerization, and provide improved molecular probes with better-defined properties for the design of future experiments.</div>
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