IDENTIFICATION OF CLEAVAGE SITES INVOLVED IN PROTEOLYTIC PROCESSING OF PSEUDOMONAS-AERUGINOSA PREPROELASTASE

被引:26
作者
KESSLER, E [1 ]
SAFRIN, M [1 ]
PERETZ, M [1 ]
BURSTEIN, Y [1 ]
机构
[1] WEIZMANN INST SCI,DEPT ORGAN CHEM,IL-76100 REHOVOT,ISRAEL
关键词
PROTEOLYTIC PROCESSING; PREPROELASTASE PROCESSING; ELASTASE; PSEUDOMONAS-AERUGINOSA;
D O I
10.1016/0014-5793(92)80134-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The extracellular elastase (33 kDa) of Pseudomonas aeruginosa is synthesized as a 53.6 kDa preproenzyme containing a long, N-terminal propeptide. The free propeptide and the elastase precursor generated upon propeptide removal were isolated from P. aeruginosa cells and subjected to N-terminal amino acid sequence analysis. The results identified Ala-174 and Ala+1 as the amino terminal residues of the propeptide and the elastase precursor, respectively, indicating that: (1) the signal peptide consists of 23 amino acid residues and its molecular weight is 2.4 kDa, (2) the propeptide contains 174 amino acid residues and is of 18.1 kDa molecular weight, and (3) no additional N-terminal proteolytic cleavage is required for elastase maturation.
引用
收藏
页码:291 / 293
页数:3
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