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Żabka M.♦, Leśniak W.♦, Prus W.♦, Kuźnicki J.♦, Filipek A.♦, Sgt1 has co-chaperone properties and is up-regulated by heat shock,
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, ISSN: 0006-291X, DOI: 10.1016/j.bbrc.2008.03.055, Vol.370, pp.179-183, 2008 Streszczenie:
The Sgt1 protein is a binding partner of heat shock proteins such as Hsp90, Hsp70 or Hsc70. In this work we show that the level of Sgt1 is increased in HEp-2 cells exposed to heat shock or radicicol. The citrate synthase aggregation assay shows that Sgt1 attenuates aggregation of the enzyme induced by increased temperature as efficiently as p23, a known co-chaperone of Hsp90. We have cloned two fragments of the human Sgt1 gene promoter (−708/+98 and −351/+98) into pGL3-luciferase vector and found that both fragments generated a 2-fold increase in luciferase activity upon heat shock. Furthermore, electrophoretic mobility shift assay revealed binding of the HSF-1 transcription factor to the heat shock element in the proximal (−42/−2) Sgt1 gene promoter fragment. These results indicate that Sgt1 is a co-chaperone protein with an expression pattern matching that of the well known heat shock proteins. Słowa kluczowe:
Sgt1, Heat shock, Radicicol, Sgt1 gene promoter, HSF-1, Co-chaperone Afiliacje autorów:
| Żabka M. | - | inna afiliacja | | Leśniak W. | - | inna afiliacja | | Prus W. | - | inna afiliacja | | Kuźnicki J. | - | inna afiliacja | | Filipek A. | - | Nencki Institute of Experimental Biology, Polish Academy of Sciences (PL) |
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