期刊
SCIENCE
卷 345, 期 6193, 页码 220-222出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1254522
关键词
-
资金
- American Heart Association
- National Institutes of Health (NIH) [F32GM103056, R01GM100951, R01AI099144, R01GM76710]
Peptidoglycan (PG) is a polysaccharide matrix that protects bacteria from osmotic lysis. Inhibition of its biogenesis is a proven strategy for killing bacteria with antibiotics. The assembly of PG requires disaccharide-pentapeptide building blocks attached to a polyisoprene lipid carrier called lipid II. Although the stages of lipid II synthesis are known, the identity of the essential flippase that translocates it across the cytoplasmic membrane for PG polymerization is unclear. We developed an assay for lipid II flippase activity and used a chemical genetic strategy to rapidly and specifically block flippase function. We combined these approaches to demonstrate that MurJ is the lipid II flippase in Escherichia coli.
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