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首页> 外文期刊>Biochemistry >DISTINCT PHOSPHATE BACKBONE CONTACTS REVEALED BY SOME MUTANT PEPTIDES OF ZINC FINGER PROTEIN SP1 - EFFECT OF PROTEIN-INDUCED BENDING ON DNA RECOGNITION
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DISTINCT PHOSPHATE BACKBONE CONTACTS REVEALED BY SOME MUTANT PEPTIDES OF ZINC FINGER PROTEIN SP1 - EFFECT OF PROTEIN-INDUCED BENDING ON DNA RECOGNITION

机译：锌指蛋白SP1的某些突变肽揭示的明显的磷酸酯骨干接触-蛋白诱导的弯曲对DNA识别的影响

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摘要

By using some mutant peptides of transcription factor Sp1, phosphate backbone contacts with the DNA binding protein containing three zinc fingers have been investigated by alkylation interference, circular permutation, DNase I footprinting, and methylation protection methods. The ethylation interference analyses of Sp1(R565S) and Sp1(K595S) mutants demonstrate that arginine at 565 position and lysine at 595 position interact with the phosphate between G(3) and G(4) and with the phosphate between G(9) and G(10) in GC-box DNA, respectively. On the basis of the experimental results for Sp1(K535G), Sp1(537-623), and Sp1(530-623), lysine and glutamine at 535 and 536 positions have been clarified to be in contacts with phosphate between G(7) and G(8) and with phosphate outside GC-box, respectively. In particular, glutamine at the N-terminal side of zinc finger 1 is a key amino acid residue to induce DNA bending and also participates in total base specificity of Sp1. The present study strongly indicates that (1) each zinc finger is not independent for the DNA interaction with Sp1 and (2) DNA base recognition of the zinc finger protein is influenced by local conformational change of DNA induced by the protein binding.
机译：通过使用转录因子Sp1的某些突变肽，已通过烷基化干扰，环状置换，DNase I足迹和甲基化保护方法研究了磷酸骨架与包含三个锌指的DNA结合蛋白的接触。 Sp1（R565S）和Sp1（K595S）突变体的乙基化干扰分析表明，在565位的精氨酸和在595位的赖氨酸与G（3）和G（4）之间的磷酸盐以及与G（9）和G（9）之间的磷酸盐相互作用。 G（10）分别在GC盒DNA中。根据Sp1（K535G），Sp1（537-623）和Sp1（530-623）的实验结果，已确认535和536位的赖氨酸和谷氨酰胺与G（7）之间的磷酸盐接触和G（8）并分别在GC盒外添加磷酸盐。特别地，锌指1的N末端侧的谷氨酰胺是诱导DNA弯曲的关键氨基酸残基，并且还参与Sp1的总碱基特异性。本研究有力地表明：（1）每个锌指并不独立于与Sp1的DNA相互作用，（2）锌指蛋白的DNA碱基识别受蛋白质结合诱导的DNA局部构象变化的影响。

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