Detection of proteins that bind to the leucine zipper motif of c-Myb.
The product of the c-myb proto-oncogene, c-Myb, binds DNA and can enhance transcription of genes bearing copies of the DNA sequence it recognises. Deletion or disruption of a negative regulatory domain (NRD) in the carboxyl portion of c-Myb results in enhanced transactivating capacity and in parallel, leads to activation of its ability to transform haemopoietic cells. Since mutational analysis has shown that one critical element within the NRD is a leucine zipper motif, we have sought to identify cellular proteins that can interact with the c-Myb leucine zipper. Using fusion proteins containing this region as an affinity reagent, we have identified two nuclear proteins, p67 and p160, that bind to the wild-type, but not to a mutated c-Myb leucine zipper. These two proteins were shown to be related by comparison of peptides generated by partial digestion. While p160 was found to be ubiquitous amongst different murine haemopoietic cell lines, and was also present in NIH3T3 fibroblasts, p67 was detected in a restricted set of immature myeloid cells. Intriguingly p160, but not p67, could also bind to the c-Jun leucine zipper.
Favier
D
D
Hanson Centre for Cancer Research, Adelaide, South Australia.
Gonda
T J
TJ
D000595:Amino Acid Sequence; D001483:Base Sequence; D002352:Carrier Proteins / Q000032:analysis*; D002460:Cell Line; D002467:Cell Nucleus / Q000737:chemistry; D006801:Humans; D016350:Leucine Zippers; D008969:Molecular Sequence Data; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins / Q000235:genetics*; D020598:Proto-Oncogene Proteins c-myb; D011519:Proto-Oncogenes; D012680:Sensitivity and Specificity
D002352:Carrier Proteins; C000715470:MAS1 protein, human; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins; D020598:Proto-Oncogene Proteins c-myb