Grothe S, Krogsrud R L, McClellan D J, Milner J L, Wood J M
J Bacteriol. 1986 Apr;166(1):253-9. doi: 10.1128/jb.166.1.253-259.1986.
Proline is accumulated in Escherichia coli via two active transport systems, proline porter I (PPI) and PPII. In our experiments, PPI was insensitive to catabolite repression and was reduced in activity twofold when bacteria were subjected to amino acid-limited growth. PPII, which has a lower affinity for proline than PPI, was induced by tryptophan-limited growth. PPII activity was elevated in bacteria that were subjected to osmotic stress during growth or the transport measurement. Neither PPI nor uptake of serine or glutamine was affected by osmotic stress. Mutation proU205, which was similar in genetic map location and phenotype to other proU mutations isolated in E. coli and Salmonella typhimurium, influenced the sensitivity of the bacteria to the toxic proline analogs azetidine-2-carboxylate and 3,4-dehydroproline, the proline requirements of auxotrophs, and the osmoprotective effect of proline. This mutation did not influence proline uptake via PPI or PPII. A very low uptake activity (6% of the PPII activity) observed in osmotically stressed bacteria lacking PPI and PPII was not observed when the proU205 lesion was introduced.
脯氨酸通过两种主动转运系统在大肠杆菌中积累,即脯氨酸转运蛋白I(PPI)和PPII。在我们的实验中,PPI对分解代谢物阻遏不敏感,当细菌处于氨基酸限制生长时,其活性降低两倍。PPII对脯氨酸的亲和力低于PPI,它由色氨酸限制生长诱导。在生长或转运测量过程中受到渗透胁迫的细菌中,PPII活性升高。PPI以及丝氨酸或谷氨酰胺的摄取均不受渗透胁迫影响。proU205突变在遗传图谱位置和表型上与在大肠杆菌和鼠伤寒沙门氏菌中分离出的其他proU突变相似,它影响细菌对有毒脯氨酸类似物氮杂环丁烷-2-羧酸和3,4-脱氢脯氨酸的敏感性、营养缺陷型对脯氨酸的需求以及脯氨酸的渗透保护作用。该突变不影响通过PPI或PPII摄取脯氨酸。当引入proU205损伤时,在缺乏PPI和PPII的渗透胁迫细菌中观察到的极低摄取活性(PPII活性的6%)未出现。