Targeting of muralytic enzymes to the cell division site of Gram-positive bacteria:: repeat domains direct autolysin to the equatorial surface ring of Staphylococcus aureus

被引:102
作者
Baba, T [1 ]
Schneewind, O [1 ]
机构
[1] Univ Calif Los Angeles, Sch Med, Dept Microbiol & Immunol, Los Angeles, CA 90095 USA
关键词
amidase; autolysin; equatorial surface ring; glucosaminidase; Staphylococcus aureus;
D O I
10.1093/emboj/17.16.4639
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
Staphylococcus aureus secretes autolysin (Atl) to complete cell division by hydrolyzing its thick cell wall layer at a designated site, known as the equatorial surface ring. Secreted pro-Atl (1256 amino acids) is cleaved at residues 198 and 775 to generate a propeptide, amidase and glucosaminidase, respectively. Here we examined the mechanism that directs amidase and glucosaminidase to the cell division site on the staphylococcal surface. Targeting of pro-Atl to the cell surface occurred prior to its proteolytic processing, Three repeat domains (RI, R2 and R3) located at the center of pro-Atl are necessary and sufficient for the targeting of reporter proteins to the equatorial surface ring, Pro-Atl cleavage at residue 775 separates the polypeptide such that R1 and R2 are linked to the C-terminus of amidase, whereas R3 is located at the N-terminus of glucosaminidase, Thus, it appears that the repeat domains direct pro-Atl, amidase and glucosaminidase to a specific receptor at the equatorial surface ring of staphylococci, thereby allowing localized peptidoglycan hydrolysis and separation of the dividing cells.
引用
收藏
页码:4639 / 4646
页数:8
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