TRANSACTIVATION AND TRANSFORMATION BY MYB ARE NEGATIVELY REGULATED BY A LEUCINE-ZIPPER STRUCTURE

被引:120
作者
KANEIISHII, C
MACMILLAN, EM
NOMURA, T
SARAI, A
RAMSAY, RG
AIMOTO, S
ISHII, S
GONDA, TJ
机构
[1] INST PHYS & CHEM RES,TSUKUBA LIFE SCI CTR,TSUKUBA,IBARAKI 305,JAPAN
[2] INST MED & VET SCI,HANSON CTR CANC RES,ADELAIDE,SA 5000,AUSTRALIA
[3] OSAKA UNIV,INST PROT RES,SUITA,OSAKA 565,JAPAN
[4] ROYAL MELBOURNE HOSP,LUDWIG INST CANC RES,TUMOR BIOL BRANCH,PARKVILLE,VIC 3050,AUSTRALIA
关键词
ONCOGENE; DNA-BINDING PROTEIN; NEGATIVE REGULATORY DOMAIN; POINT MUTANTS; INHIBITORS;
D O I
10.1073/pnas.89.7.3088
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The negative regulatory domain of the c-myb protooncogene product (c-Myb) normally represses transcriptional activation by c-Myb. We show here that a leucine-zipper structure is a component of the negative regulatory domain, because its disruption markedly increases both the transactivating and transforming capacities of c-Myb. We also demonstrate that this leucine-zipper structure can interact with cellular proteins. Our results suggest that an inhibitor that suppresses transactivation binds to c-Myb through the leucine zipper and that c-Myb can be oncogenically activated by missense mutation.
引用
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页码:3088 / 3092
页数:5
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