THE HEXAPEPTIDE LFPWMR IN HOXB-8 IS REQUIRED FOR COOPERATIVE DNA-BINDING WITH PBX1 AND PBX2 PROTEINS

被引:99
作者
NEUTEBOOM, STC
PELTENBURG, LTC
VANDIJK, MA
MURRE, C
机构
[1] Department of Biology, 0366 Univ. of California at S. Diego, San Diego
[2] Department of Immunology, University Hospital Utrecht
关键词
D O I
10.1073/pnas.92.20.9166
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 Hox gene products are DNA-binding proteins, containing a homeodomain, which function as a class of master control proteins establishing the body plan in organisms as diverse as Drosophila and vertebrates, Hox proteins have recently been shown to bind cooperatively to DNA with another class of homeodomain proteins that include extradenticle, Pbx1, and Pbx2, Hox gene products contain a highly conserved hexapeptide connected by a linker of variable length to the homeodomain, We show that the hexapeptide and the linker region are required for cooperativity with Pbx1 and Pbx2 proteins, Many of the conserved residues present in the Hoxb-8 hexapeptide are required to modulate the DNA binding of the Pbx proteins, Position of the hexapeptide relative to the homeodomain is important, Although deletions of two and four residues of the linker peptide still show cooperative DNA binding, removal of all six linker residues strongly reduces cooperativity. In addition, an insertion of 10 residues within the linker peptide significantly lowers cooperative DNA binding, These results show that the hexapeptide and the position of the hexapeptide relative to the homeodomain are important determinants to allow cooperative DNA binding involving Hox and Pbx gene products.
引用
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页码:9166 / 9170
页数:5
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