MULTIPLE OLIGOMERIC STATES REGULATE THE DNA-BINDING OF HELIX-LOOP-HELIX PEPTIDES

被引:98
作者
FAIRMAN, R
BERANSTEED, RK
ANTHONYCAHILL, SJ
LEAR, JD
STAFFORD, WF
DEGRADO, WF
BENFIELD, PA
BRENNER, SL
机构
[1] DUPONT MERCK PHARMACEUT CO,EXPTL STN,POB 80328,WILMINGTON,DE 19880
[2] BOSTON BIOMED RES INST,DEPT MUSCLE RES,BOSTON,MA 02114
关键词
D O I
10.1073/pnas.90.22.10429
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
To study the protein-protein interactions that allow Id, a negative regulator of cell differentiation, to inhibit the DNA-binding activities of MyoD and E47, we have synthesized peptides corresponding to the helix-loop-helix domains of MyoD, E47, and Id. We show that Id preferentially inhibits the sequence-specific DNA-binding activity of MyoD, a muscle-specific protein, as compared to E47, a more ubiquitous protein. The Id helix-loop-helix domain itself forms stable tetramers, and its inhibitory activity arises from the formation of a heterotetrameric structure with MyoD. The formation of this higher order complex provides a general mechanism by which inhibitory proteins can generate sufficient interaction free energy to overcome the large DNA-binding free energy of dimeric DNA-binding proteins.
引用
收藏
页码:10429 / 10433
页数:5
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