Co-immunoprecipitation of Hsp101 with cytosolic Hsc70
In animals and yeast, cytosolic Hsp70s function in concert with other molecular chaperones. Hsp70 is a major chaperone in the Hsp90 multi-chaperone complexes that participate in maturation of steroid receptors and several other proteins. Hsp70s also appear to form a complex with Hsp90 and Hsp110/sHs...
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 43(2005), 1 vom: 28. Jan., Seite 13-8 |
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| Format: | Aufsatz |
| Sprache: | English |
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2005
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| Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
| Schlagworte: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. HSP101 protein, plant HSP70 Heat-Shock Proteins Plant Proteins Transcription Factors Adenosine Triphosphate 8L70Q75FXE Lactalbumin 9013-90-5 mehr... |
| Zusammenfassung: | In animals and yeast, cytosolic Hsp70s function in concert with other molecular chaperones. Hsp70 is a major chaperone in the Hsp90 multi-chaperone complexes that participate in maturation of steroid receptors and several other proteins. Hsp70s also appear to form a complex with Hsp90 and Hsp110/sHsp. A 100 kDa protein was co-immunoprecipitated with cytosolic Hsc70 from maize seedlings (Zea mays). The presence of this complex was further confirmed using gel-filtration chromatography. Mass spectrometric analysis showed that the 100 kDa protein is homologous with Arabidopsis Hsp101. Treatment with apyrase enhanced the co-immunoprecipitation of Hsp101 with Hsc70, while ATP had the opposite effect. In the presence of carboxymethylated alpha-lactalbumin (CMLA), which is permanently unfolded, the complex dissociated. Based on these observations, it is concluded that Hsc70 and Hsp101 are present in a complex in the plant cytosol |
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| Beschreibung: | Date Completed 04.05.2005 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2690 |