Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in Staphylococcal peptidoglycan pentaglycine side chain formation
Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in Staphylococcal peptidoglycan pentaglycine side chain formation
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DOI：
10.1128/jb.179.23.7573-7576.1997
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发表时间：
1997-12-01
影响因子：
3.2
通讯作者：
Labischinski, H
中科院分区：
文献类型：
--
作者：
Ehlert, K;Schroder, W;Labischinski, H
femAB操纵子编码两个几乎相同的类似于50 kDa的蛋白质，参与葡萄球菌五甘氨酸肽间桥的形成。通过化学诱变和选择溶葡萄球菌酶抗性分离的突变体的femA区域的测序和分析揭示了导致截短的FemA蛋白表达的点突变。这些femA突变体，虽然仍然产生一个完整的FemB，表现出相同的表型所描述的femAB双突变体。因此，FemA似乎是必不可少的添加甘氨酸残基2和3只，而FemB是参与专门的甘氨酸残基4和5的附件。虽然FemB与FemA有39%的同一性，但它不能取代FemA。FemA和FemB蛋白似乎对它们所连接的甘氨酸残基的位置具有高度特异性。
The femAB operon codes for two nearly identical similar to 50-kDa proteins involved in the formation of the staphylococcal pentaglycine interpeptide bridge. Sequencing and analysis of the femA region of mutants isolated by chemical mutagenesis and selection for lysostaphin resistance revealed point mutations leading to the expression of truncated FemA proteins. These femA mutants, although still producing an intact FemB, exhibited a phenotype identical as that described for femAB double mutants. Thus, FemA seems to be essential for the addition of glycine residues 2 and 3 only, whereas FemB is involved in the attachment of exclusively glycine residues 4 and 5. Although FemB has 39% identity with FemA, it cannot substitute for FemA. The FemA and FemB proteins seem to be highly specific in regard to the position of the glycine residues that they attach.