1. Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells
- Author
-
Maki Murata-Hori, Mizuki Hino, Masa Aki Okubo, Hiroshi Hosoya, and Kazuki Kurogi
- Subjects
endocrine system ,animal structures ,Immunoprecipitation ,Molecular Sequence Data ,Biophysics ,Mitosis ,urologic and male genital diseases ,Biochemistry ,Microtubules ,HeLa ,Microtubule ,Tubulin ,Immunoscreening ,Heat shock protein ,Humans ,Amino Acid Sequence ,Fluorescent Antibody Technique, Indirect ,Molecular Biology ,Heat-Shock Proteins ,Microscopy, Confocal ,biology ,Sequence Homology, Amino Acid ,Antibodies, Monoclonal ,Cell Biology ,biology.organism_classification ,Molecular biology ,Precipitin Tests ,Cell biology ,Spindle apparatus ,embryonic structures ,biology.protein ,HeLa Cells ,Protein Binding - Abstract
One of the monoclonal antibodies raised against mitotic HeLa cells (termed as mH3) recognized a 27-kDa protein and stained microtubules in the mitotic spindles of HeLa cells. Immunoscreening of a HeLa cDNA library revealed that mH3 antigen is a small heat shock protein, HSP27. Immunoprecipitation analysis using mH3 suggested that both α- and β-tubulin are associated with HSP27. Further, sucrose-cushioned ultra centrifugation revealed that HSP27 is co-sedimented with taxol-stabilized microtubules. These results indicate that HSP27 associates with tubulin/microtubules in HeLa cells.
- Published
- 2000