TSP - A TAIL-SPECIFIC PROTEASE THAT SELECTIVELY DEGRADES PROTEINS WITH NONPOLAR-C TERMINI

被引:167
作者
SILBER, KR
KEILER, KC
SAUER, RT
机构
[1] Department of Biology, Massachusetts Inst. of Technology, Cambridge
关键词
ESCHERICHIA-COLI; HYDROPHOBIC TAIL; LAMBDA-REPRESSOR; PROTEIN SEQUENCE HOMOLOGY;
D O I
10.1073/pnas.89.1.295
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
An Escherichia coli protease designated Tsp (tail-specific protease) has been purified, and its gene has been cloned and sequenced. Tsp specifically degrades a variant of the N-terminal domain of lambda-repressor in which the rive C-terminal residues, which are polar in wild type, have been replaced by nonpolar residues. This substrate specificity in vitro parallels the previously reported selective degradation in vivo of N-terminal-domain variants with nonpolar C-terminal residues. The gene sequence and N-terminal protein sequence of Tsp predict a protein of 660 amino acids. The deduced protein sequence of Tsp shows no significant homology to known protease sequences but does show sequence similarity to the human and bovine interphotoreceptor retinoid-binding proteins, which bind hydrophobic ligands.
引用
收藏
页码:295 / 299
页数:5
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