DNA-BINDING PROPERTIES OF THE PURIFIED ANTENNAPEDIA HOMEODOMAIN

被引：188

作者：

AFFOLTER, M ^{[1
]}

PERCIVALSMITH, A ^{[1
]}

MULLER, M ^{[1
]}

LEUPIN, W ^{[1
]}

GEHRING, WJ ^{[1
]}

机构：

[1] HOFFMANN LA ROCHE CIE AG,CH-4002 BASEL,SWITZERLAND

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 11期

关键词：

Helix-turn-helix;

D O I：

10.1073/pnas.87.11.4093

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 in vitro DNA binding properties of a purified 68-amino acid Antennapedia homeodomain (Antp HD) peptide have been analyzed. Equilibrium and kinetic binding studies showed that stable DNA-protein complexes are formed with a Kd of 1.6 × 10-9 M and 1.8 × 10-10 M, respectively. Heterodimer analysis led to the conclusion that Antp HD interacts in vitro as a monomer with the DNA target sites used in our study. The results of methylation and ethylation interference studies indicated that the Antp HD closely approaches the target DNA primarily from one side in a region extending across three phosphate backbones. The DNA binding properties of the HD and prokaryotic DNA binding domains that share a helix-turn-helix motif are compared. (.

引用

页码：4093 / 4097

页数：5

共 36 条

[1] RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE-434 - A VIEW AT HIGH-RESOLUTION [J].