嗜热厌氧菌热纤维梭菌中的氨基酸转运由电化学钠梯度驱动。
Amino acid transport in the thermophilic anaerobe Clostridium fervidus is driven by an electrochemical sodium gradient.
作者信息
Speelmans G, Poolman B, Konings W N
机构信息
Department of Microbiology, University of Groningen, Haren, The Netherlands.
出版信息
J Bacteriol. 1993 Apr;175(7):2060-6. doi: 10.1128/jb.175.7.2060-2066.1993.
Abstract
Amino acid transport was studied in membranes of the peptidolytic, thermophilic, anaerobic bacterium Clostridium fervidus. Uptake of the negatively charged amino acid L-glutamate, the neutral amino acid L-serine, and the positively charged amino acid L-arginine was examined in membrane vesicles fused with cytochrome c-containing liposomes. Artificial ion diffusion gradients were also applied to establish the specific driving forces for the individual amino acid transport systems. Each amino acid was driven by the delta psi and delta mu Na+/F and not by the Z delta pH. The Na+ stoichiometry was estimated from the amino acid-dependent 22Na+ efflux and Na(+)-dependent 3H-amino acid efflux. Serine and arginine were symported with 1 Na+ and glutamate with 2 Na+. C. fervidus membranes contain Na+/Na+ exchange activity, but Na+/H+ exchange activity could not be demonstrated.
摘要
对嗜热厌氧解肽细菌热纤维梭菌的细胞膜中的氨基酸转运进行了研究。在与含细胞色素c的脂质体融合的膜囊泡中检测了带负电荷的氨基酸L-谷氨酸、中性氨基酸L-丝氨酸和带正电荷的氨基酸L-精氨酸的摄取。还应用人工离子扩散梯度来确定各个氨基酸转运系统的特定驱动力。每种氨基酸由Δψ和ΔμNa⁺/F驱动，而非由ZΔpH驱动。通过氨基酸依赖性²²Na⁺外流和Na⁺依赖性³H-氨基酸外流估算Na⁺化学计量。丝氨酸和精氨酸与1个Na⁺同向转运，谷氨酸与2个Na⁺同向转运。热纤维梭菌细胞膜含有Na⁺/Na⁺交换活性，但未证实有Na⁺/H⁺交换活性。
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