TI  - Elimination of false negative results in the two-hybrid system in the
      phagocyte <prot>NADPH oxidase</prot>.
PG  - 301-5
AB  - The yeast two-hybrid system is finding increased use in the study of
      interactions between proteins. In this method, two polypeptides are
      expressed in yeast as fusion proteins to a transcriptional activator
      DNA-binding domain (bd) and activating domain (ad), respectively.
      Interaction between the two polypeptides reconstitutes function of a
      transactivator which controls expression of reporters. The phagocyte  <prot>NADPH 
      oxidase</prot> is a complex of membrane <prot>cytochrome b558</prot> (comprised of subunits
       <prot>p22-phox</prot>  and  <prot>gp91-phox</prot> ) and three cytosol proteins ( <prot>p47-phox</prot> ,  <prot>p67-phox</prot> ,
      and  <prot>p21rac</prot> ) that translocate to membrane and bind to  <prot>cytochrome b558</prot> . This
      is the first report to demonstrate that two of cytosolic components of
      <prot>cytochrome b558</prot>,  <prot>p47-phox</prot>  binding to  <prot>p67-phox</prot>  each other. We encountered
      several methodological problems in the two-hybrid system which are the
      focus of this report.
AD  - Graduate Institute of Biochemistry, Kaohsiung Medical College, Taiwan,
