TI  - Reconstitution of the multiprotein complex of  <prot>pp60src</prot> ,  <prot>hsp90</prot>,  and  <prot>p50</prot>  in a
      cell-free system.
PG  - 2902-8
AB  - A rabbit reticulocyte lysate system that has been used to reconstitute
      functional complexes between steroid receptors and the 90-kDa heat shock
      protein (<prot>hsp90</prot>) has been used here to form complexes between the  <prot>pp60src</prot>
      tyrosine kinase  and  <prot>hsp90</prot> . Reticulocyte lysate forms complexes between
       <prot>hsp90</prot>  and a temperature-sensitive mutant of Rous sarcoma virus  <prot>pp60v-src</prot> ,
      which is normally present in cytosol virtually entirely in the
      multiprotein complex form. In addition,   <prot>hsp90</prot>   in the lysate complexes with
      wild-type  <prot>pp60v-src</prot> , of which only a small portion is normally recovered
      in cytosol in the native multiprotein complex, and with the cellular
      homolog,  <prot>pp60c-src</prot> , which has never been recovered in cytosol in the form
      of a native multiprotein complex with <prot>hsp90</prot>. Moreover, the reticulocyte
      lysate-reconstituted complex also contains the 50-kDa phosphoprotein
      component of the native <prot>pp60v-src</prot> multiprotein complex. The native and
      reconstituted  <prot>pp60src</prot> - <prot>hsp90</prot>  complexes have similar thermal stability and,
      like steroid receptor heterocomplexes, they are stabilized by molybdate.
      As previously shown with reticulocyte lysate-reconstituted steroid
      receptor heteroprotein complexes, the reconstituted  <prot>pp60src</prot>  multiprotein
      complex contains  <prot>hsp70</prot> , which is a major candidate for providing the
      protein unfoldase activity required for <prot>hsp90</prot> association.
AD  - Department of Pharmacology, University of Michigan Medical School, Ann
