Atkinson Steve, Chang Chien-Yi, Sockett R Elizabeth, Cámara Miguel, Williams Paul
Institute of Infections, Immunity and Inflammation, Centre for Biomolecular Science, University of Nottingham, Nottingham NG7 2RD, United Kingdom.
J Bacteriol. 2006 Feb;188(4):1451-61. doi: 10.1128/JB.188.4.1451-1461.2006.
The Yersinia enterocolitica LuxI homologue YenI directs the synthesis of N-3-(oxohexanoyl)homoserine lactone (3-oxo-C6-HSL) and N-hexanoylhomoserine lactone (C6-HSL). In a Y. enterocolitica yenI mutant, swimming motility is temporally delayed while swarming motility is abolished. Since both swimming and swarming are flagellum dependent, we purified the flagellin protein from the parent and yenI mutant. Electrophoresis revealed that in contrast to the parent strain, the yenI mutant grown for 17 h at 26 degrees C lacked the 45-kDa flagellin protein FleB. Reverse transcription-PCR indicated that while mutation of yenI had no effect on yenR, flhDC (the motility master regulator) or fliA (the flagellar sigma factor) expression, fleB (the flagellin structural gene) was down-regulated. Since 3-oxo-C6-HSL and C6-HSL did not restore swimming or swarming in the yenI mutant, we reexamined the N-acylhomoserine lactone (AHL) profile of Y. enterocolitica. Using AHL biosensors and mass spectrometry, we identified three additional AHLs synthesized via YenI: N-(3-oxodecanoyl)homoserine lactone, N-(3-oxododecanoyl)homoserine lactone (3-oxo-C12-HSL), and N-(3-oxotetradecanoyl)homoserine lactone. However, none of the long-chain AHLs either alone or in combination with the short-chain AHLs restored swarming or swimming in the yenI mutant. By investigating the transport of radiolabeled 3-oxo-C12-HSL and by introducing an AHL biosensor into the yenI mutant we demonstrate that the inability of exogenous AHLs to restore motility to the yenI mutant is not related to a lack of AHL uptake. However, both AHL synthesis and motility were restored by complementation of the yenI mutant with a plasmid-borne copy of yenI.
小肠结肠炎耶尔森菌的LuxI同源物YenI指导N-3-(氧代己酰基)高丝氨酸内酯(3-氧代-C6-HSL)和N-己酰基高丝氨酸内酯(C6-HSL)的合成。在小肠结肠炎耶尔森菌yenI突变体中,游动运动在时间上延迟,而群体运动则被消除。由于游动和群体运动都依赖鞭毛,我们从亲本和yenI突变体中纯化了鞭毛蛋白。电泳显示,与亲本菌株相比,在26℃下培养17小时的yenI突变体缺乏45 kDa的鞭毛蛋白FleB。逆转录PCR表明,虽然yenI突变对yenR、flhDC(运动主调节因子)或fliA(鞭毛σ因子)的表达没有影响,但fleB(鞭毛蛋白结构基因)被下调。由于3-氧代-C6-HSL和C6-HSL不能恢复yenI突变体的游动或群体运动,我们重新检查了小肠结肠炎耶尔森菌的N-酰基高丝氨酸内酯(AHL)谱。使用AHL生物传感器和质谱,我们鉴定出另外三种通过YenI合成的AHL:N-(3-氧代癸酰基)高丝氨酸内酯、N-(3-氧代十二酰基)高丝氨酸内酯(3-氧代-C12-HSL)和N-(3-氧代十四酰基)高丝氨酸内酯。然而,单独的长链AHL或与短链AHL组合都不能恢复yenI突变体的群体运动或游动运动。通过研究放射性标记的3-氧代-C12-HSL的转运,并将AHL生物传感器引入yenI突变体,我们证明外源AHL不能恢复yenI突变体的运动能力与AHL摄取不足无关。然而,通过用携带质粒的yenI拷贝对yenI突变体进行互补,AHL合成和运动能力都得到了恢复。