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...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 43(2005), 1 vom: 28. Jan., Seite 13-8
1. Verfasser: Zhang, Chun (VerfasserIn)
Weitere Verfasser: Guy, Charles L
Format: Aufsatz
Sprache:English
Veröffentlicht: 2005
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... Apyrase EC 3.6.1.5
LEADER 01000naa a22002652 4500
001 NLM154178322
003 DE-627
005 20231223065502.0
007 tu
008 231223s2005 xx ||||| 00| ||eng c
028 5 2 |a pubmed24n0514.xml 
035 |a (DE-627)NLM154178322 
035 |a (NLM)15763661 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Zhang, Chun  |e verfasserin  |4 aut 
245 1 0 |a Co-immunoprecipitation of Hsp101 with cytosolic Hsc70 
264 1 |c 2005 
336 |a Text  |b txt  |2 rdacontent 
337 |a ohne Hilfsmittel zu benutzen  |b n  |2 rdamedia 
338 |a Band  |b nc  |2 rdacarrier 
500 |a Date Completed 04.05.2005 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 7 |a HSP101 protein, plant  |2 NLM 
650 7 |a HSP70 Heat-Shock Proteins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Transcription Factors  |2 NLM 
650 7 |a Adenosine Triphosphate  |2 NLM 
650 7 |a 8L70Q75FXE  |2 NLM 
650 7 |a Lactalbumin  |2 NLM 
650 7 |a 9013-90-5  |2 NLM 
650 7 |a Apyrase  |2 NLM 
650 7 |a EC 3.6.1.5  |2 NLM 
700 1 |a Guy, Charles L  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 43(2005), 1 vom: 28. Jan., Seite 13-8  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:43  |g year:2005  |g number:1  |g day:28  |g month:01  |g pages:13-8 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 43  |j 2005  |e 1  |b 28  |c 01  |h 13-8